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Author Topic: Enzyme therapy?
spookydew
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Hello,

Has anyone tried or studied enzyme therapy?

Seems impressive.

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spookydew
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Do enzymes breakdown the protein of spirochetes?

If not still seems beneficial in illness as it would breakdown and replenish vitamins and minerals and maybe boosting the immune system.

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Kayda
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I know a chiropractor who said enzyme therapy will work against anything including Lyme. I could see it working in the gut but wonder about deeper tissues.

Kayda

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luvs2ride
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My doctor diagnosed leaky gut. Enzymes are necessary to help break down proteins. When our immune systems are knocked down and our gut is damaged, partially digested foods escape into our bodies and create a lot of illness.

He has had me on 2 different enzymes since April. Vitalzym (12 capsules daily between meals). Similase 1 capsule 3x daily with meals.

Also L-Glutamine and amino acids. Pure Synergy Supergreen powder, CoQ10 enzyme 3x daily, liver support.

I am thriving.

Luvs

--------------------
When the Power of Love overcomes the Love of Power, there will be Peace.

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Meg
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spooky-

Search the posts of Kathy Boss member #3062~~

Large amounts of enzymes taken after other treatments....

--------------------
Success Stories---Treatment Guidelines

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spookydew
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Meg,
I can't find those posts on Kathy. Only finding trip to Europe for fragmin shots and hyperbaric treatments.

I see that she used some enzyme supplements. But has anyone used the raw diet and enzyme therapy?

Does anyone know anyone with chronic illness that got better doing this?

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pq
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Abstracts on borrelia, mentioning enzymes that can be bought otc. ; e.g.: chymotrypsin, trypsin and their effect on borrelia.

Elastase, which kills Bb is found in small amounts in the otc product, pancreatin(this comes from hogs). chymotrypsin, and trypsin are also in pancreatin.
The salt and vitamin c regime is supposed to trigger elastase release.


elastase can be bought otc, but imo, is too dangerous to take, esp. in moderate to high doses.

i left out the titles of some abstracts due to some technical difficulties getting them out of the "box-fields" they were encased in, so i just posted the abstract itself with attendant pmids so they can still be found on medline.

J Immunol. 1988 Jan 1;140(1):265-72.


* Benach JL,
* Coleman JL,
* Golightly MG.
State of New York Department of Health, Stony Brook 11794.
A hybridoma cell line formed by the fusion of the P3x63-Ag8.653 myeloma cell line with splenocytes from BALB/c mice immunized with Borrelia burgdorferi produced an IgM monoclonal antibody (mAb-11G1) with kappa-light chains which detected an antigenic determinant in a major spirochetal protein of m.w. approximately 31,000, also known as outer surface protein A (OSP-A). Apparent saturation was reached in approximately 35 min with 34 ng of mAb-11G1 binding to 5 X 10(7) spirochetes giving an estimated 4.8 X 10(2) IgM molecules per spirochete and thus a minimum of 480 binding sites per organism. Enzymatic digestion studies suggest that the antigenic determinant to mAb-11G1 is contained within the peptide chain of OSP-A as binding could be eliminated by treatment of the spirochetes with proteinase K, Pronase and pepsin (100 to 200 micrograms/ml of enzyme) but not by trypsin or bromelain treatment. Periodate oxidation as well as mixed and endoglycosidase treatment of the spirochetes did not alter the binding of mAb-11G1. Two-dimensional gel electrophoresis of whole spirochetal cell lysates disclosed that OSP-A is a heterogeneously charged basic protein with an apparent isoelectric point range from 8.5 to 9.0. Amino acid analysis of OSP-A showed a 10% lysine component which could provide the basic nature to the protein. OSP-A with the intact antigenic determinant for mAb-11G1 can be found in the urine of hamsters experimentally infected with B. burgdorferi.
PMID: 2447170

* Lusitani D,
* Malawista SE,
* Montgomery RR.
Department of Internal Medicine, Yale University School of Medicine, New Haven, Connecticut 06520-8031, USA.
The killing of Borrelia burgdorferi by intact human polymorphonuclear leukocytes (PMNL) and by individual PMNL components was compared. Intact PMNL killed B. burgdorferi 6.5-fold more efficiently and 5-fold more completely when spirochetes were opsonized with specific antibodies. U-cytoplasts, which have activatable oxidase, killed opsonized B. burgdorferi with an efficiency similar to that of intact PMNL in killing unopsonized B. burgdorferi. Although B. burgdorferi were susceptible to H(2)O(2) and nitric oxide, PMNL lysates killed B. burgdorferi nearly as well as intact PMNL killed opsonized B. burgdorferi, suggesting a critical role for granule contents. B. burgdorferi were killed by the PMNL antimicrobial components elastase, LL-37, bactericidal/permeability-increasing protein, and human neutrophil peptide-1. B. burgdorferi had limited susceptibility to killing by lysozyme and were not killed by azurocidin, proteinase 3, or lactoferrin. The efficient killing of B. burgdorferi by a variety of PMNL mechanisms highlights the paradoxical persistence of spirochetes in vivo.
PMID: 11920297

* Garcia R,
* Gusmani L,
* Murgia R,
* Guarnaccia C,
* Cinco M,
* Rottini G.
International Centre for Genetic Engineering and Biotechnology, Trieste, Italy. [email protected]
Phagocytosis of Borrelia burgdorferi by human polymorphonuclear leukocytes triggers oxygen-dependent and -independent mechanisms of potentially cidal outcome. Nevertheless, no factor or process has yet been singled out as being borreliacidal. We have studied the B. burgdorferi-killing ability of the myeloperoxidase-H2O2-chloride system and that of primary and secondary granule components in an in vitro assay. We found that neither secondary granule acid extracts nor the chlorinating system could kill these microorganisms, while primary granule extracts were effective. The Borrelia-killing factor was purified to homogeneity and demonstrated to be elastase. Its cidal activity was found to be independent of its proteolytic activity.
PMID: 9529060
* Barbour AG,
* Barrera O,
* Judd RC.
Borrelia hermsii undergoes spontaneous antigenic variation in vivo and in vitro. Serotype specificity is associated with expression of one of a family of molecular weight-variable proteins, the pI proteins. We studied the structure of the pI proteins as well as the molecular weight-invariable pII proteins of three serotypes of B. hermsii HS1: C, 7, and 21. The techniques used were one-dimensional (1-D) mapping of Staphylococcus aureus V8 protease-generated peptides and two-dimensional (2-D) mapping of alpha-chymotrypsin-generated peptides. The pI and pII proteins were isolated by excision of polypeptides from stained polyacrylamide gel electropherograms. The 1-D peptide patterns were visualized by fluorography of intrinsically [14C]leucine-labeled proteins or by silver stain. Before 2-D mapping, polypeptides in excised gel fragments were labeled with 125I in the presence of chloramine-T. We also compared the 2-D peptide maps of pI proteins, pI7 and pI21, after their surface-exposed portions were radioiodinated using 1,3,4,6-tetrachloro-3 alpha,6 alpha-diphenylglycoluril (Iodogen). The I-D and 2-D peptide maps demonstrated the following: (a) pI proteins of the three serotypes have few V8 protease- or chymotrypsin-generated peptides in common, and (b) pI proteins of each serotype appear to be identical. The findings suggest that pI protein variability derives from extensive differences in the amino acid sequences of these proteins.
PMID: 6644241
* Katona LI,
* Ayalew S,
* Coleman JL,
* Benach JL.
Department of Molecular Genetics, State University of New York, Stony Brook, NY 11794, USA. [email protected]
mAb CB2, directed against outer surface protein B (OspB), causes bacteriolysis of Borrelia burgdorferi in the absence of complement. How this happens is unknown. We examined the effect of mAb binding on OspB tertiary structure by using limited proteolysis to probe changes in protein conformation. Truncated OspB (tOspB) that lacked N-terminal lipid was cleaved by four enzymes: trypsin, endoproteinase Arg-C, endoproteinase Asp-N, and endoproteinase Glu-C. CB2 affected the cleavage by trypsin and Arg-C, but not by AspN or Glu-C. None of the enzymes cleaved CB2 under these conditions. Both trypsin and Arg-C cleaved tOspB near the N-terminus; CB2 slowed the rate of cleavage, but did not affect the identity of the sites cleaved. Irrelevant mAb had no effect, indicating that the effect was specific. CB2 was active against tOspB of strain B31, but not against tOspB of strain BEP4, to which it does not bind, suggesting that binding was required to elicit the effect on cleavage. With trypsin, CB2 showed a maximal effect at 8 mol of tOspB to 1 mol of mAb. At this ratio, not enough CB2 was present to bind all the tOspB; therefore, either CB2 shows turnover or CB2 acts by binding tOspB and effecting a change in this tOspB such that it, in turn, propagates the effect in other molecules of tOspB. Regardless of the mechanism, these data show that CB2 elicits a change in tOspB that can be measured by its reduced susceptibility to protease cleavage.
PMID: 10640758

Title: Mapping the major antigenic domains of the native flagellar antigen of Borrelia burgdorferi.
Authors: Jiang W, Luft BJ, Schubach W, Dattwyler RJ, Gorevic PD
Source: J Clin Microbiol 1992 Jun;30(6):1535-40
Organization: Department of Medicine State University of New York Stony Brook 11794-8161.

Abstract:
Purified flagellar protein (p41) of Borrelia burgdorferi (strain B31) was subjected to chemical cleavage with hydroxylamine or proteolysis with V8 protease, endoproteinase Asp-N, or alpha-chymotrypsin. The resulting polypeptides were identified by sodium dodecyl sulfate- polyacrylamide gel electrophoresis, and their positions in the published DNA sequence of the p41 protein were determined by amino- terminal sequencing and amino acid analysis. Epitope specificities of antibody binding by a monoclonal antibody raised by immunization of mice with purified flagella and pooled sera from patients with multiple erythema migrans, late Lyme borreliosis, or secondary syphilis were analyzed by Western blots (immunoblots) of peptides transferred to Immobilon polyvinylidene difluoride filters. The major epitope binding one murine monoclonal antibody (158) was localized to a carboxy-terminal domain that includes residues 300 to 336. The dominant epitopes binding human polyclonal antibodies are in the central portion of the molecule (residues 182 to 218) that is not conserved compared with other bacterial flagellins. Additional reactive epitopes were identified in the amino-terminal domain of the protein. Sera from patients with syphilis bound strongly to the amino- terminal conserved domain, providing a structural basis for cross- reactivity seen in standard enzyme-linked immunosorbent assays, but not to the central part of the molecule. Specific and cross-reactive antigenic determinants need to be considered in the design of improved immunodiagnostics for spirochetal diseases.

Keywords:
Amino Acid Sequence, Antibodies, Bacterial, IM, Antibodies, Monoclonal, Antigenic Determinants, IM, Antigens, Bacterial, IM, Blotting, Western, Borrelia burgdorferi, IM, Flagella, IM, Human, Molecular Sequence Data, Peptide Mapping, Support, Non-U.S. Gov't, Medline File

Language: German

Unique ID: 92325211

* Moroni A,
* Sambri V,
* Massaria F,
* La Placa M Jr,
* Brocchi E,
* De Simone F,
* Cevenini R.
Istituto di Microbiologia, University of Bologna, Italy.
The differential cleavage of surface proteins of Borrelia burgdorferi IRS strains by several proteases was examined. Proteinase K, trypsin, chymotrypsin and thermolysin all cleaved the outer surface protein B (OspB) to undetectable levels by Coomassie Brilliant Blue staining, whereas some residual protein was detected by immunoblotting with polyclonal and monoclonal antibodies. Not even antigenic fragments were detectable by immunoblotting with 1A8 monoclonal antibody reactive with OspB. Less effective or ineffective was the cleavage of OspB by V8 protease and proteinase A, respectively. The outer surface protein A was cleaved only by proteinase K. The effect of trypsin on borreliae viability and adhesion to cultured cells was also studied. The trypsin treatment of borreliae did not impair the viability of organisms which continued to synthesize the cleaved OspB. The attachment of B. burgdorferi to HEp-2 cells was reduced by 41% after treatment with trypsin, whereas preincubation of borreliae with monoclonal antibody 1A8 and guinea pig immune serum reduced the adhesion of borreliae to the cells by 32% and 87%, respectively.
PMID: 1602994
* Bunikis J,
* Barbour AG.
Departments of Microbiology & Molecular Genetics and Medicine, University of California Irvine, Irvine, California 92697, USA.
The outer membrane of Borrelia burgdorferi, the Lyme disease agent, contains lipoproteins anchored by their lipid moieties and integral proteins with membrane-spanning regions. We used the techniques of in situ proteolysis, immunofluorescence, in vitro growth inhibition, and cross-linking with formaldehyde to characterize topological relationships between P66, an integral membrane protein, and selected Osp lipoproteins of B. burgdorferi. Protease treatment of intact spirochetes cleaved P66 and Osp proteins but not the periplasmic flagellin or the BmpA protein of the cytoplasmic membrane.
P66 of cells lacking OspA, OspB, and OspC was more susceptible to trypsin cleavage than was P66 of cells with these Osp proteins. A monoclonal antibody against the surface loop of P66 bound, agglutinated, and inhibited the growth of viable spirochetes lacking OspA, OspB, OspC, and OspD but not of the cells that expressed OspA, OspC, and/or OspD. When cells were fixed, the antibody bound to cells that express OspD and OspC but still not to cells with OspA. The close association of OspA and P66 was confirmed by the crosslinking of the two proteins by formaldehyde. These results show that Osp proteins, particularly OspA, limit the access of antibody or trypsin to the surface loop region of P66. The proximity and possible contact between P66 and OspA (or other Osp proteins) may hinder the effectiveness of antibodies to what otherwise would be an appropriate vaccine target.
PMID: 10338494

[ 02. January 2007, 07:10 PM: Message edited by: pq ]

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Kayda
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WHy are you citing Stony Brook? That's where Wormser works! They've been bad news for Chronic Lyme patients.

I don't understand.

Kayda

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spookydew
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Pq,

Too much and too over my brain ability to digest or break down right now. Please simplify.

What about the raw food diet for the enzyme activity? Could that put my body in healthy state and improve immune function?

Thanks for the info.

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pq
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spooky,

just copy to a word file, split up each abstract in to "digestible" passages, and read at your leisure.

you don't have to understand every sentence, and concept in these to see the potential use of enzymes for lyme, and, perhaps other tbds.

the main points are that some of the enzymes used in research can be purchased otc, and that, by extension, imply that they can be used to attack borrelia, by taking them----in vivo.

there are many links, and essays on enzymes i could have posted, but instead i posted these in the service of trying to get a "laser-like" focus on borrelia with the use of these enzymes.

again scan these to find chymotrypsin, trypsin, elastase, etc.

theoretically, if researchers are using otc enzymes in their in vitro work, then by implication, they should work in vivo.

[ 01. January 2007, 05:02 PM: Message edited by: pq ]

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spookydew
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Sorry,
I have had a three second goldfish memory for I don't even remember how many years.

I keep forgetting what I want to say in my post when I post.

In searching the internet, looks like enzymes could restore health by shrinking cancer tumors, reversing allergies and mcs (the latter being my interest), and after I leave the sites I can't remember what else improves or cures. Must be the brain damage neuro talked about.

Anyway, Is this more snake oil?


Happy New Year everyone in case I forget later!

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pq
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re-read my post cause i edited it.
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spookydew
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I went to doctor of osteopathic medicine in Cincinatti once who offered me enzyme potentiated desensitization for severe allergies and mcs. Not approved FDA in USA. However, could order the injections from England.

Seemed impressive but carried many restrictions and anaphyllactic dangers. I have history of anaphyllaxis reactions and too restrictive for my work schedule.

I suppose raw diet and enzyme supplements would be mildly similar to enzyme potentiate desensitization.

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pq
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http://www.betterhealthinternational.com/nattozyme.asp

here is one passage by a person with one or more insect-borne infections'':

`` bromelain and natto are enzymes which dissolves coagulation deposits which
potentially could cause herxing. Bromelain was found to potentate
antibiotics sufficiently that anti-biotic resistant infections responded to
antibiotics.''


''If you are feeling sluggish, it is likely that your own immune system is now
able to attack the infection that had been hidden behind the coagulation
deposits and are producing (slowly) die off toxins from killing the
infections (aka herx). You will likely feel most sluggish about 1-4 hrs
after taking them...''

''Our practice was to take such just before bedtime -- it improved sleep and
you herx well you sleep -- often waking up feeling better (from improved
sleep and reduced infection levels).''
________________________________________________________

More specifically, here are abstracts on chymotrypsin and borrelia.

* Jiang W,
* Luft BJ,
* Schubach W,
* Dattwyler RJ,
* Gorevic PD.
Department of Medicine, State University of New York, Stony Brook 11794-8161.
Purified flagellar protein (p41) of Borrelia burgdorferi (strain B31) was subjected to chemical cleavage with hydroxylamine or proteolysis with V8 protease, endoproteinase Asp-N, or alpha-chymotrypsin. The resulting polypeptides were identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and their positions in the published DNA sequence of the p41 protein were determined by amino-terminal sequencing and amino acid analysis. Epitope specificities of antibody binding by a monoclonal antibody raised by immunization of mice with purified flagella and pooled sera from patients with multiple erythema migrans, late Lyme borreliosis, or secondary syphilis were analyzed by Western blots (immunoblots) of peptides transferred to Immobilon polyvinylidene difluoride filters. The major epitope binding one murine monoclonal antibody (158) was localized to a carboxy-terminal domain that includes residues 300 to 336. The dominant epitopes binding human polyclonal antibodies are in the central portion of the molecule (residues 182 to 218) that is not conserved compared with other bacterial flagellins. Additional reactive epitopes were identified in the amino-terminal domain of the protein. Sera from patients with syphilis bound strongly to the amino-terminal conserved domain, providing a structural basis for cross-reactivity seen in standard enzyme-linked immunosorbent assays, but not to the central part of the molecule. Specific and cross-reactive antigenic determinants need to be considered in the design of improved immunodiagnostics for spirochetal diseases.


PMID: 1378061
* Sambri V,
* Moroni A,
* Massaria F,
* Brocchi E,
* De Simone F,
* Cevenini R.
Institute of Microbiology, University of Bologna, S. Orsola Hospital, Italy.
The presence of a low molecular mass polypeptidic antigen in Borrelia burgdorferi was described. The protein was exposed at the bacterial surface since it was clearly identified by mAb 3H4 using the immunofluorescence test performed with living bacteria. This antigen was cleaved by proteinase K treatment, whereas it was resistant to the action of chymotrypsin, trypsin and thermolysin. Western blotting analysis of the immunological reactivity of this antigenic structure performed using monoclonal antibody, mouse-immune ascitic fluids raised against B. burgdorferi and other spirochetes, sera from patients with Lyme disease and other infirmities in which false positive results in serological tests for B. burgdorferi have been described, demonstrated that this protein expresses only species-specific epitopes which may be recognized during human B. burgdorferi infections.
PMID: 172595


* Barbour AG,
* Barrera O,
* Judd RC.
Borrelia hermsii undergoes spontaneous antigenic variation in vivo and in vitro. Serotype specificity is associated with expression of one of a family of molecular weight-variable proteins, the pI proteins. We studied the structure of the pI proteins as well as the molecular weight-invariable pII proteins of three serotypes of B. hermsii HS1: C, 7, and 21. The techniques used were one-dimensional (1-D) mapping of Staphylococcus aureus V8 protease-generated peptides and two-dimensional (2-D) mapping of alpha-chymotrypsin-generated peptides. The pI and pII proteins were isolated by excision of polypeptides from stained polyacrylamide gel electropherograms. The 1-D peptide patterns were visualized by fluorography of intrinsically [14C]leucine-labeled proteins or by silver stain. Before 2-D mapping, polypeptides in excised gel fragments were labeled with 125I in the presence of chloramine-T. We also compared the 2-D peptide maps of pI proteins, pI7 and pI21, after their surface-exposed portions were radioiodinated using 1,3,4,6-tetrachloro-3 alpha,6 alpha-diphenylglycoluril (Iodogen). The I-D and 2-D peptide maps demonstrated the following: (a) pI proteins of the three serotypes have few V8 protease- or chymotrypsin-generated peptides in common, and (b) pI proteins of each serotype appear to be identical. The findings suggest that pI protein variability derives from extensive differences in the amino acid sequences of these proteins.
PMID: 6644241

-----------------------------------------------
The effect of trypsin on borrelia:

* Moroni A,
* Sambri V,
* Massaria F,
* La Placa M Jr,
* Brocchi E,
* De Simone F,
* Cevenini R.
Istituto di Microbiologia, University of Bologna, Italy.
The differential cleavage of surface proteins of Borrelia burgdorferi IRS strains by several proteases was examined. Proteinase K, trypsin, chymotrypsin and thermolysin all cleaved the outer surface protein B (OspB) to undetectable levels by Coomassie Brilliant Blue staining, whereas some residual protein was detected by immunoblotting with polyclonal and monoclonal antibodies. Not even antigenic fragments were detectable by immunoblotting with 1A8 monoclonal antibody reactive with OspB.

Less effective or ineffective was the cleavage of OspB by V8 protease and proteinase A, respectively. The outer surface protein A was cleaved only by proteinase K. The effect of trypsin on borreliae viability and adhesion to cultured cells was also studied. The trypsin treatment of borreliae did not impair the viability of organisms which continued to synthesize the cleaved OspB. The attachment of B. burgdorferi to HEp-2 cells was reduced by 41% after treatment with trypsin, whereas preincubation of borreliae with monoclonal antibody 1A8 and guinea pig immune serum reduced the adhesion of borreliae to the cells by 32% and 87%, respectively. PMID: 1602994

[ 01. January 2007, 12:18 AM: Message edited by: pq ]

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pq
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on antibiotics and enzymes , here are two abstracts. these two abstracts are on seratiopeptidase.

[Article in Japanese]
* Aratani H,
* Tateishi H,
* Negita S.
1) A focal infection was prepared by inoculation of staphylococci into rat gingiva. Then, concentrations in oral tissues (gingiva, tongue and masseter), serum and liver of the infected rats which were given ciclacillin, ampicillin, cephalexin and minocycline in a dose of 100 mg/kg p.o. were investigated and effects of serratiopeptidase (20 mg/kg) on these concentrations were studied.
2) Concentrations of ciclacillin in the oral tissues were approximately 10% of a serum level. A gingival concentration was elevated 8.5-fold by pretreatment with serratiopeptidase. A concentration in infected gingiva was 2.5-fold of that of another side of gingiva.
3) Concentrations of ampicillin in the oral tissues were approximately 15% of a serum level. A gingival concentration was elevated 5.7-fold by pretreatment with serratiopeptidase. A concentration in infected gingiva ws 2.2-fold of that of another side of gingiva.
4) Concentrations of cephalexin in the oral tissues were approximately 3 to 5-fold of a serum level except that in masseter. A gingival concentration was slightly elevated (1.1-fold) by pretreatment with serratiopeptidase. A concentration in infected gingiva was 1.7-fold of that of another side of gingiva.
5) Concentrations of minocycline in the oral tissues were 1.3 to 7.2-fold of a serum level. A gingival concentration was elevated 2.2-fold by pretreatment with serratipeptidase. A concentration in infected gingiva was 3.1-fold of that of another side of gingiva.
6) Gingival concentrations of antibiotics were higher than those of tongue and masseter and serratiopeptidase elevated gingival concentrations.
PMID: 7001087


* Okumura H,
* Watanabe R,
* Kotoura Y,
* Nakane Y,
* Tangiku O.
Studies were performed in 8 patients with osteoarticular infections to examine the concentrations of sulbenicillin in the venous blood and exudate following administration and the concentrations of the antibiotic in the exudate when serratiopeptidase was orally administered concomitantly with the antibiotic. The results of the examination indicated that the transfer of sulbenicillin into the exudate tended to increase when 30 mg/day of serratiopeptidase was concomitantly given for 6 days, though further examination was thought necessary by increasing number of subjects and elaborating on the methodology.
PMID: 853579

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spookydew
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The info impressive to me.

Thanks pq!

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pq
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some stuff on bromelain and antibiotics:

copy and breakup into digestible passages.


Bromelain

Potentiation of Antibiotics
Antibiotic potentiation is one of the primary
uses of bromelain in several foreign
countries. Bromelain can modify the permeability
of organs and tissues to different drugs.
It prolongs sleeping time in mice administered
pentobarbital30 and increases spinal levels of
penicillin and gentamycin in rats. In humans,
bromelain has been documented to increase
blood and urine levels of antibiotics16 and results
in higher blood and tissue levels of tetracycline
and amoxycillin when they are administered
concurrently with bromelain.31
Treatment of 18 women with 80 mg of
bromelain concurrently with amoxycillin or
tetracyclin resulted in increased serum levels
and concentrations of both antibiotics in uterus,
ovarian tubes, and ovaries as compared with
controls. This effect was not generated by indomethacin,
an anti-inflammatory drug which
acts as a cyclooxygenase inhibitor, which indicates
that bromelain has some undetermined
activity that enhances absorption and tissue
distribution of antibiotics.32

A three-fold increase
in the level of tetracycline in serum after
oral ingestion of 540 mg of entericallycoated
bromelain has also been demonstrated
in a double blind test.33


Combined bromelain and antibiotic with the following conditions; pneumonia,
bronchitis, cutaneous staphylococcus infection,
thrombophlebitis, cellulitis, pyelonephritis
and perirectal and rectal abscesses.
Twenty three of the patients had been on antibiotic
therapy without success. Bromelain was
administered four times a day along with the
following antibiotics either alone or in combination;
penicillin, chloramphenicol, erythromycin
or novobiacin.

A control group of 56
patients was treated with antibiotics alone. Of
the 23 patients who had been unsuccessfully
treated with antibiotics, 22 responded favorably
to the combined treatment. In every disease
state studied there was a significant reduction
in morbidity when the combination of
bromelain and antibiotics was used as opposed
to antibiotics alone. Another group of 106
cases was treated with bromelain alone, with
results comparable to those obtained with antibiotic
treatment.34

Forty eight patients with acute sinusitis
were placed on standard therapy, which included
antihistamines and analgesic agents,
along with antibiotics if indicated. Twenty
three of the patients received bromelain four
times daily, while the remaining 25 received a
placebo.

Of the patients receiving bromelain,
83% had complete resolution of nasal mucosal
inflammation compared with only 52% in the
placebo group. Improvement in breathing occurred
in 78% of those receiving bromelain as
compared to 68% in those receiving placebo.


In the patients not receiving antibiotic treatment,
85% of patients receiving bromelain had
complete resolution of inflammation of the
nasal mucosa and complete resolution of
breathing difficulties. Only 40% of the placebo
group had a similar outcome with respect to
inflammation, while 53% reported resolution
of breathing difficulty.35


The potentiation of antibiotics and
other medicines by bromelain may be due to
enhanced absorption, as well as increased
permeability of the diseased tissue which
enhances the access of the antibiotic to the
site of the infection. It is also thought that
the use of bromelain may provide a similar
access to specific and non-specific components
of the immune system, therefore,
enhancing the body's utilization of its own
healing resources.
Alternative Medicine Review Volume 1, Number 4
------------------------

Cardiovascular plaque is comprised basically of two components. There is the mineral component that can be removed using EDTA as an Anionic Surfactant, and there is a fibrous component that some enzymes are able to disassemble.

For over 20 years, the American biochemist, Dr. Steven Taussig, of Honolulu, has been studying the biological effects of the enzyme mixture bromelaine. This enzyme complex -- it consists of an entire group of distinct enzymes -- is obtained from the middle third of the pineapple root. It can also be obtained from the green, unripe pineapple in large quantities.

These bromelaines are able to degrade certain internal substances which may cause infarction (the so-called Prostaglandins E2 and thromboxane), thereby reducing the risk of cardiac infarction and the tendency to heart muscle necrosis, as well as simultaneously eliminating any heart pain. Also, Chinese researchers at the University of Iowa have shown that the supply of bromelaine can mobilize deposits in the blood vessels, and carry them off.

Thus, by intensive, long-term therapy with bromelaine, it is possible to "clean out" the coronary arteries from the inside. From the biological point of view, this certainly is a much more intelligent therapy than a bypass operation.

In the same manner, it is possible, by supplying larger, continuous doses of bromelaine, to dissolve deposits in the aorta and in leg arteries, as well as thrombosis residues, thus saving many a leg from amputation and even restoring them to normal functioning. The German enzyme preparation "Wobenzyme" is of particular effect in this "pipe cleaning."

The pineapple enzyme bromelaine (not bromelin!), which is absorbed into the bloodstream, can be used without limitation, is as effective eight years later as on the first day, dissolves already existing clots and cleans blood vessel walls, as well as the blood cells already mentioned. "Anavit F3" and "Ananase " are standardized bromelaine preparations. "Wobenzyme" also belongs in this group, even though it must be taken in higher doses. Magnesium, which can be bound to the membranes, such as magnesium aspartate, orotate and citrate, has a strong thrombosis-inhibiting effect. Orthodox medicine, as a rule, does not offer it. Wobenzyme is a very funny invention. It appears most desirable to have pancreatin absorbed into the blood stream since it rather specifically attacks cancer cells, as well as fibrin layers, clots and fresh thromboses.
Unfortunately, pancreatin is not resorbed. It will mainly stay in the intestine for the acknowledged purpose of digestion. Attempts to infuse pancreatin intravenously have largely failed because of poor tolerance and even shock.

In contrast to animal-derived enzymes like pancreatin, plant-derived enzymes like bromelaine (from pineapple) are easily resorbed. If bromelaine and pancreatin are administered in a fixed combination, astonishingly, a part of the pancreatin will appear in the blood stream ! A possible explanation for this is that the presence of one enzyme (the bromelaine) will neutralize the electrical properties of the other enzyme (pancreatin) and thus transiently do away with the blocking mechanism, which normally prevents the passage from the intestine into the blood.

The pineapple enzyme bromelaine is highly effective in the deactivation of antibodies and prostaglandin E-2 . Thus it is also no wonder that the bromelaine are unusually effective in the treatment of chronic rheumatism. Anavit F-3, and Ananase 100 and Wobenzyme are the names of these preparations. Already in the 18th century, the windjammer captains reported on the excellent antirheumatic-effect of the juice from the pineapple root and the green pineapple fruit. By the way, the juice from green, unripe pineapple is very effective abortifacient.

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pq
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a nattokinase-containing product called, rutozym, gave me a jump in mental speed and clarity.

i attribute this only to the nattokinase, since in the past i've taken the other 2-3 enzymes in the product, but without the nattokinase, and did not get this subtle but very distinct, effect.

http://www.mucos.de is the link for articles on trials of different enzyme-combintations---wobenzyme, wobe-mugos, phlogenzym.
the same company sells rutozym which is for the cardiovascular system, i believe, but check.

rechts-regulat is another enzyme prep, with which i haven't much experience. i only did one bottle of it, but had food in my stomach. so i can't say i gave this a fair chance to work.

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pq
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On Lumbrokinase, which i've yet to try.

http://www.allergyresearchgroup.com/proddesc/category/specprod.htm#lumbro


http://www.canadarna.com/Boluoke_chart.htm
http://www.allergyresearchgroup.com/proddesc/category/specprod.htm#lumbro


Lumbrokinase is an enzyme derived from earthworms Lumbricus rubellus. Research has shown that lumbrokinase may support healthy coagulation of blood within normal levels and enhance fibrinolytic activity, i.e. similar to nattokinase.*
&&Lumbrokinase (LK) consists of a group of proteolytic enzymes including plasminogen activator and plasmin extracted from a specific species of earthworm.
The plasminogen activator (e-PA) in LK is similar to tissue plasminogen activator (t-PA) from other sources, which makes it possible to show the thrombolytic activity only in the presence of fibrin. Therefore, LK has the advantage of not causing excessive bleeding. The activity of LK is much higher than most traditional Chinese products that are available in the United States. Four phases of clinical studies have been done on LK at the Beijing Xuanwu Hospital (the top hospital in nerve & internal medicine in China). LK has been widely used in over 100 hospitals in Beijing since 1995. In Jakarta, LK has been used in thousands of hospitals and stores, in more than 20 provinces and cities, as well as in Hong Kong, Taiwan, Southeast Asia, and Europe.
LK is recognized by the Ministry of Public Health in China. LK capsules technology was awarded a certificate of National Significance Achievement in Science and Technology, listed as the Promotional project of National Key Technology Achievement and the National Torch Plan Program, and selected as National Key New product by six major ministries.
Each enteric-coated capsule contains:
Lumbrokinase 230 mg
Other ingredients:
Starch
Suggested use: As a dietary supplement, 1 capsule in the morning, 1 capsule in the afternoon and 2 capsules at bedtime, or as directed by a healthcare practitioner. May be taken with or without food. Take with 8-10 oz of water, with or without food. Use under medical supervision if taking anticoagulant drugs. Contraindicated in any condition associated with bleeding.

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pq
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http://www.organic-pharmacy.com/ARG.Lumbrokinase.htm

Lumbrokinase by Allergy Research Group 30 Capsules, 230 mg/cap
http://organicpharmacy.org/products/Lumbrokinase

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pq
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Or http://www.thorne.com/altmedrev/fulltext/bromelain1-4.html
" Combined bromelain and antibiotic therapy was instituted for 53
hospitalized patients with the following conditions; pneumonia, bronchitis,
cutaneous staphylococcus infection, thrombophlebitis, cellulitis,
pyelonephritis and perirectal and rectal abscesses. Twenty three of the
patients had been on antibiotic therapy without success. Bromelain was
administered four times a day along with the following antibiotics either
alone or in combination; penicillin, chloramphenicol, erythromycin or
novobiacin. A control group of 56 patients was treated with antibiotics
alone.

Of the 23 patients who had been unsuccessfully treated with
antibiotics, 22 responded favorably to the combined treatment. In every
disease state studied there was a significant reduction in morbidity when
the combination of bromelain and antibiotics was used as opposed to
antibiotics alone.
Another group of 106 cases was treated with bromelain
alone, with results comparable to those obtained with antibiotic
treatment.34"

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pq
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Nattokinase:
http://www.life-enthusiast.com/enzyme/nattokinase.htm

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pq
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antibiotics and enzymes:

The potentiators (bromelain, serrapetase etc is documented on medline).

For example, for Serrapeptase:
concentration of antibiotic in tissue increased by :

ciclacillin - 8.5 fold (850%)
ampicillin - 5.7 fold (570%)
cephalexin - 3 to 5 fold (300-500%)
minocycline - 2.2 fold (220%)

[ 01. January 2007, 03:45 PM: Message edited by: pq ]

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pq
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http://smart-nutrition.net/serrapeptase-research.htm

Wobenzym
http://www.iherb.com/store/ProductDetails.aspx?c=Herbs&pid=NTV-41178

Hypercoagulation
http://www.diagnose-me.com/cond/C546624.html

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spookydew
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Looks like I need to get some Nattokinase to help my memory.

My mother could have used the bromelain instead of the triple bypass that killed her.

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pq
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consider that some lymies have a paradoxically worsening of symptoms and signs, when taking moderate to high doseses of vitamins c, b2,and b6 that "conduce" to an increased production of quinolinic acid by brain macrophages.
quin. acid is a natural toxin.

niacin, and magnesium conduce to a temporary decrease in quinolinic acid production.

irritability, at minimum, is one manifestation of an increased quin. acid leveel in the brain.
i don't know of the other mental, and emotional manifestations of an increased production of quin. acid., but there are more than a few.


with magnesium, some, if not many lymies, initially at least, get an increase of Sx, then after a while these diminish. initially, these can be spooky, as happened to me with mag.chloride.

on niacin(b3):

b3 can be a multiple-edged sword in that large doses exasperate existing liver problems, and perhaps, heart problems, as well.
with me, i exasperated existing heart Sx with niacin >= 25mg.

increased liver enzyme levels in persons with existing liver problems. given all the abx and other meds. us lymies take, this would be a given.

initially, mag. sulfate gave me a weakening of shoulder-girdle muscles and/or nerves.
used of these two forms of magnesium after symptoms, and signs diminish, eventually disappearing---in my case. others may have a different experience.

zinc, esp. in moderate to high doses can be problematic with lymies.

i haven't read anything about the effects of other b cplx b vits., and minerals on borrelia infection, and other insect-borne infections.

consider if any of these are contributing to negative cognitive, and emotional symptoms.

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spookydew
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pq,

I only remember having good memory and cognitive skills from age 17-25. Prior to that not good and after that not good. Then at 32 the memory problems

progressed quickly. I got lost driving every time I drove. I would suddenly realize I didn't know why I was even in the car let alone where I was going.

I learned to keep driving and to not turn around because I eventually would recognize something or would remember.

Sometimes, I wouldn't know if I was going to work or going home from work.

I don't remember watching movies from one night to the next. At work If I'm destracted at all I forget what I set out to do.

One time, I forgot how to use a key to unlock something.

I started on herbs and atbs with my dx. Didn't start Vit C til last year. 2grams/day.

Spect scan - decreased perfusion right temporal lobe. MRI- one - two areas increased intensity in white matter.

They frequently think I have ms. I have pituitary sx.s. Had low acth and adh and tsh. Now normal but still carry the sx.s.

However, I have improved significantly. The constant deep seated burning ache in center of my head for 11 1/2 years left Nov. 2,2005. I

kept thinking it would be back but I guess not.
I know longer get lost driving or forget where I'm going.


Apparently, I had something working on my brain at a young age then lyme exacerbated it.

I did buy some multi enzymes and slept better than I have in a long time last night.

I did have stiff neck with pain and fever today and dizziness.

Thanks for all of the info on enzymes. It helps to know what others are doing that works.

I will get the nattokinase next week. If you have any other ideas please let me know.

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pq
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your welcome spooky,

only 4% of us have experienced, and still experience the same things as you listed; the other 96% of us don't mention it, and/or are liars(for good reason(s), too). [Big Grin]

my letter transpositions in my typing are manifestation(s), either and/or both of my infections and "drain bamage,"if any, temporary and/or permanent.

most if not all you listed will clear up with treatment, and time.

see works of brian fallon, and robert bransfield that mention many of the things you listed.

caveat: if on meds for other conditions, its best to consult with your doctor on enzyme therapy, as with the antibiotics, the enzyme(s) could make your medicine(s) for these other condition(s) work only too well, thereby causing some problems.


good luck
pq [Wink]

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spookydew
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Can these enzymes potentiate herbs?
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pq
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i'd imagine theres every conceivable interaction of effects one could think of.

check with your pharmacist for leads and links, authors, texts, reference texts, etc.

antibiotics are king,and, absent this,for the quickest,most efficious progress utilizing herbs, consider either a naturopath, or traditional chinese medicine (wo-)man experienced with insect-borne infections.

treatment of insect-borne infections, and esp. lyme, are too serious,and complicated to be playing footsy with "this, that, and the other",non-antibiotic-based therapy.

i implore you to see somebody, asap!

good luck, spooky,

pq

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