Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.4.21.1 (chymotrypsin)
10,938 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Treatment of cells grown to exponential phase with 4% sodium dodecyl sulfate for 3 h at 100 degrees C resulted in solubilization of all cellular components except for peptidoglycan. In most strains, cells cultured in liquid gonococcal broth at pH 7.2 yielded a peptidoglycan composed primarily of N-acetylmuramic acid N-acetylglucosamine, alanine, glutamic acid, and diaminopimelic acid in a molar ratio of 1:1:2:1:1. The peptidoglycan in these cells accounted for 1 to 2% (dry weight) of the cells. However, in cells cultured at pH 6.0, the dry weight of peptidoglycan increased to 4 to 13%. Preliminary investigations indicated that the apparent increase in weight is strain dependent and is due in part to associated protein(s). Neisseria gonorrhoeae strain CS7 had elevated amounts of protein associated with the peptidoglycan regardless of growth pH. The peptidoglycan-protein complex could not be dissociated by additional extraction with sodium dodecyl sulfate, 10 M LiCl2, or ethylenediaminetetraacetate or by 7.5% polyacrylamide gel electrophoresis. The complex could be degraded by lysozyme, trypsin, chymotrypsin, Pronase B, and Chalaropsis sp. muramidase.
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PMID:Cell envelope of Neisseria gonorrhoeae CS7: peptidoglycan protein complex. 3 3

Vaginal washings from women attending a veneral disease clinic were examined for the presence of protease that cleaved IgA subclass 1 (IgA1). In a crude assay, vaginal washings cleaved [125I]IgA1 in 19 of 25 specimens from individuals from whom Neisseria gonorrhoeae were cultivated. Forty-six specimens from 104 women whose cultures were negative for N. gonorrhoeae also cleaved [125I]IgA1. Vaginal washings from six of six women with culture-proven gonorrhea cleaved [125I]IgA1 into low-molecular-weight components identical to those produced by partially purified IgA1-specific protease from gonococci. The hydrolysis of [125I]IgA1 by vaginal washings from women whose cultures were negative for N. gonorrhoeae yielded cleavage products that resembled those of trypsin or alpha-chymotrypsin. These findings indicate that gonococci residing in the female genital tract produce IgA1-specific protease that can be detected in the vaginal washings of infected women.
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PMID:Studies on gonococcus infection. XVII. IgA1-cleaving protease in vaginal washings from women with gonorrhea. 10 39

The major outer membrane proteins from 10 gonococcal strains were examined after 125I-labeling of the proteins as single bands resolved by polyacrylamide gel electrophoresis in sodium dodecyl sulfate. These 125I-proteins were then treated with either trypsin or alpha-chymotrypsin, and the resultant 125I-peptides were visualized by autoradiography after two-dimensional electrophoretic and chromatographic separation on thin-layer cellulose sheets. Several 125I-peptides were present in all the major outer membrane proteins examined. The presence and absence of additional 125I-peptides segregated the major proteins into two pattern groups. One group consisted of major outer membranes with molecular weights of 34,000 or 33,000; major proteins with molecular weights of 32,000 constituted the other group. Two beta-lactamase-producing gonococcal isolates were examined. Their major outer membrane proteins were identical in apparent molecular weights and alpha-chymotryptic 125I-peptide fingerprints; these proteins contained 125I-peptides not found in other gonococcal major proteins. No 125I-peptide differences were found among the major outer membrane proteins of strain F62 gonococci that exhibited differences in piliation and/or colony opacity characteristics.
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PMID:Studies on gonococcus infection. XVIII. 125I-labeled peptide mapping of the major protein of the gonococcal cell wall outer membrane. 11 Jun 81

Proteolytic enzymes (chymotrypsin, trypsin) i.m. injections in a dose of 5 mg twice daily for 4 to 10 days were used in combined therapy of 218 patients with recurrences of gonorrhea, gonorrheal epididymitis and orchiepididymitis; 23 patients with acute orchiepididymitis were injected heparin intramuscularly in a dose of 5000 U twice daily for 7 weeks. Etiologic cure was achieved in 99.7 percent, postgonorrheal residual phenomena were detected in 5.7 percent of cases (93.9 and 17.5 percent, respectively, in a reference group). The length of treatment of a patient with gonorrhea relapse shortened by 8.6 days on an average and of that with orchiepididymitis and epididymitis by 5.9 days. Formula are presented for calculating the economic efficacy of treatment of those working and not working patients.
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PMID:[The assessment of the efficacy of introducing a new method for treating gonorrhea]. 211 40

The examination has involved 218 patients. The incidence of relapses in acute and subacute gonorrhea has made up 6.3%, 5.2% in chronic and 4.5% in complicated condition. Recurrences were observed in 5.3 days on an average after therapy of new gonorrhea cases and in 8.8 days after treatment of chronic disease. Mixed urogenital infection was recorded in 37.8% of cases; in gonorrhea eventuating in clinical cure it was observed in 24% of cases. Relapses developed in 50.2% of patients after antibiotic therapy and in 49.8% after combined treatment. A single relapse occurred in 85.6% of patients; two and more relapses in 14.4%. The disease recurred after penicillin therapy in 6.5% after aminoglycosides in 6.9%, and after tetracyclin treatment in 4.2% of cases. Therapy with proteolytic enzymes (chymotrypsin, trypsin 5 mg i.m. twice a day) combined with antibiotics resulted in etiological cure in 99.3% of patients, the incidence of postgonorrheal symptoms reduced and made up 6.8% (in the patients not administered protease this share made up 19.2%), and the length of inpatient treatment shortened by 8-14.6 days.
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PMID:[Recurrences of gonorrhea in men (the characteristics of the course and treatment)]. 219 97

The study has involved 3702 male patients with gonorrhea. Of these 62 percent were fresh cases, 38 percent chronic ones; there were 218 patients (5.9 percent) with recurrences, of these 63.3 percent with new relapses and 36.7 percent with chronic ones. 85.3 percent of patients developed monorelapses. The recurrences were equally frequent after antibiotic therapy (50.2 percent) and after combined treatment (49.8 percent). Proteolytic enzymes (chymotrypsin, trapsin 5 mg twice daily with a 12 hrs interval) in combination with an antibiotic were administered to 242 patients with gonorrhea complicated by epididymo-orchitis and with gonorrhea relapses. Etiologic cure was achieved in all of them; postgonorrheal conditions were recorded in 6-7 percent and depended on the antibiotic administered; in reference patients recurrences were recorded in 4.2-6.5 percent of cases, postgonorrheal conditions in 14-21.4 percent of cases. Enzymic therapy helped reduce the length of inpatient therapy of a patient by 5.93 days on an average in cases with orchidoepididymitis and by 14.64 days in gonorrhea relapses, with the economic effect per worker being 131.4 and 307.2 rubles, respectively.
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PMID:[The sociomedical efficacy of the enzyme therapy of gonorrhea patients]. 225 66

Whole bacteria, isolated outer membranes, and purified protein I (PI) from one transparent (O-) and two different opaque (O+) phenotype gonococcal strains (serogroups I, II, and III; PI serotypes 1, 5, and 9b) were each treated with tolylsulfonyl phenylalanyl chloromethyl ketone-trypsin, alpha-chymotrypsin, and proteinase K. Protein IA (PIA) of strain 7122 (O-, serotype 1, serogroup I) was resistant to proteolysis by tolysulfonyl phenylalanyl chloromethyl ketone-trypsin and alpha-chymotrypsin and only slightly affected by proteinase K, as long as it was associated with intact bacteria or isolated outer membranes. Purified PIA however was cleaved by these enzymes, resulting in two to five fragments. In contrast, all preparations of strains 5766 opaque phenotype (O+, serotype 7, serogroup II) and 1955 (O+, serotype 9b, serogroup III) were accessible to proteolysis, resulting in cleavage fragments of PIB compatible to those described previously by O. Barrera and J. Swanson (Infect. Immun. 44:565-568, 1984), M. S. Blake et al. (Infect. Immun. 33:212-222, 1981), and Blake (in G. K. Schoolnik, ed., The Pathogenic Neisseriae, 1985). Our data indicated that the purified PIB fraction was more accessible to proteases than the PIBs of whole bacteria or outer membranes. The fragmentation pattern of PIA cleavage products were quite different from PIB fragments, consistent with the different structure of these two groups of PI molecules. Time-dependent cleavage experiments with proteases, i.e., alpha-chymotrypsin, indicated that PIA was subsequently cleaved into smaller fragments. Highly reactive monoclonal antibodies, each specific for a surface-exposed epitope of PIA of strain 7122 or PIB of strains 5766 and 1955, as assessed by coagglutination, Western blot, and immunofluorescence, were reacted with PIA and PIB cleavage fragments in Western blot experiments. All cleavage fragments of the purified PIA and PIB preparations with molecular weights of greater than or equal to 14,200 showed immune reaction in Western blotting, whereas whole cell and outer membrane PIB fragments were less reactive with the specific monoclonal antibodies.
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PMID:Surface-exposed antigenic cleavage fragments of Neisseria gonorrhoeae proteins 1A and IB. 309 94

Monoclonal antibodies (Mab) with specificity for protein I (PI) from Neisseria gonorrhoeae (GC) were examined for bactericidal activity. Mab 4G5 (gamma 3), ID3 (gamma 2a), and 1G6 (gamma 2a) bound to surface-exposed epitopes on PI of GC strain R11 (IA serotype) as assessed by co-agglutination and 125I protein A uptake. Mab 2H1 (gamma 3) that were directed against IB serotype strains and Mab 2E9 (gamma 2a) were negative in co-agglutination and protein A uptake assays and served as controls for some experiments. Only 4G5 and 1D3 were bactericidal for R11 when presensitized organisms were incubated in 10% absorbed, pooled normal human serum (PNHS) or 10% hypogammaglobulinemic serum (H gamma S) despite binding of nearly equivalent numbers of 4G5, 1D3, and 1G6 to R11 during presensitization, as assessed by 125I-protein A uptake. These Mab activated complement to a similar extent on GC R11, leading to deposition of 56.4 X 10(3), 61.9 X 1093), and 47.1 X 10(3) molecules of C3/organism during incubation in 10% C8-deficient serum. Deposition occurred almost exclusively via the classical complement pathway. Measurement of complement component C9 binding to R11 during incubation in H gamma S showed 35,700 molecules of C9/organism with 4G5, 32,600 C9/organism with 1D3, and surprisingly, 29,600 C9/organism with 1G6. Eight thousand four hundred molecules of C9/organism bound to 2E9-coated organisms, 6000 C9/organism to 2H1-coated bacteria, and 3600 C9/organism to nonpresensitized organisms. The C5b-9 complex deposited by 4G5 had a different sedimentation profile by sucrose density gradient analysis from the C5b-9 complex deposited by 1G6, consistent with a different molecular configuration of the bound complex. Mab 1G6 and 1D3, but not 2E9 or 2H1, were able to compete with 125I-4G5 for binding to GC R11. A Mab (2E6) directed against protein III of GC competed weakly with 125I-4G5 for binding to GC R11. Mab 1G6, but not 1D3, blocked 4G5-dependent killing in a dose-related fashion. Both 4G5 and IG6 reacted weakly with native PI of GC R11 by immunoblotting, but neither Mab recognized the 34,800 m.w. fragment of PI generated by trypsin and chymotrypsin treatment of outer membranes. In contrast, 2E9 reacted strongly by immunoblot with both native and cleaved PI of GC R11, suggesting binding to buried determinants of PI. These experiments show that Mab directed against identical or closely associated, surface-exposed epitopes on gonococcal PI differ markedly in bactericidal activity, despite leading to deposition of nearly equivalent numbers of C3 and C9 molecules per organism.
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PMID:Monoclonal antibodies directed against gonococcal protein I vary in bactericidal activity. 392 Mar 19

The association of in vitro human leukocytes with pilated, type 2 Neisseria gonorrhoeae exceeds that for nonpilated, type 4 organisms but is less than that for nonpilated, type 4(*) gonococci. The two nonpilated forms of gonococci (types 4 and 4(*)) attach to tissue culture cells to a much lesser extent than do pilated, type 2 organisms of the same strain. Trypsin treatment of either pilated (type 2) or nonpilated (type 4(*)) gonococci markedly reduces the attachment-ingestion of these organisms with leukocytes, but the same trypsin treatment does not depilate the type 2 organisms nor visibly alter the morphology of their pili. Similar reductions in association with leukocytes are found if the gonococci are pretreated with chymotrypsin, heat, or glutaraldehyde. High levels of association between gonococci and leukocytes are reestablished if the trypsin or chymotrypsin-treated organisms are reincubated in protease-free medium. These data suggest that interactions between gonococci and human neutrophils are mediated through surface characteristics of the bacteria, different from those which influence attachment of the organisms to tissue culture cells. In the latter instance, pili appear to positively influence gonococcal attachment, whereas in the former a nonpilus bacterial cell wall nonpilus protein is probably the major determiner in the interaction between leukocytes and gonococci.
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PMID:Studies on gonococcus infection. V. Observations on in vitro interactions of gonococci and human neutrophils. 421 76

Proteolytic enzymes inhibit the growth of some strains and opacity variants of Neisseria gonorrhoeae. To understand the inhibitory effects of these enzymes, we examined several strains to determine the actions of proteases on the three predominant proteins in gonococcal outer membranes. namely, the major outer membrane protein (protein I), the sometimes-expressed opaque protein (protein II), and protein III. In a comparison of the protein I species expressed by different strains, we observed a pattern based on subunit molecular weight and susceptibility to enzymatic degradation. Protein I species having molecular weights of 34,000 were more susceptible to proteolysis, whereas protein I species having molecular weights of 33,000 were less susceptible, and protein I species having molecular weights of 32,000 were resistant. This pattern was observed both in intact cells and in purified outer membranes. All of the enzymes degraded protein II, but this susceptibility appeared to be influenced in part by the species of protein I present. Protein III was resistant to all of the proteolytic enzymes tested. Based on the resulting fragments from each proteolytic cleavage of proteins I and II and their membrane associations, we suggest how these proteins may be arranged in intact membranes. Our data suggested the presence of an endogenous gonococcal enzyme. This enzyme appeared to degrade proteins I and II into fragments resembling the fragments resulting from the action of chymotrypsin.
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PMID:Effects of proteolytic enzymes on the outer membrane proteins of Neisseria gonorrhoeae. 679 Apr 41


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