Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.4 (trypsin)
 42,187 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

An antigen (ZAB) common to Neisseria gonorrhoeae was prepared by stepwise elution of a crude gonococcal antigen (ZA) from columns of diethylaminoethyl cellulose employing 0.02 M phosphate buffers, pH 7.6, containing increasing concentrations of sodium chloride. Rats immunized with ZAB produced reaginic (IgE) antibody which cross-reacted with ZA prepared from eight gonococcal strains by the passive cutaneous anaphylaxis (PCA) test. Heating of the sera at 56 degrees C for 4 h destroyed the PCA activity. The PCA activity of the anti-ZAB rat serum was removed after absorption with ZAB antigen or with rabbit anti-rat IgE but not after absorption with gonococcal lipopolysaccharide or with heat-killed or formalinized gonococci. Treatment of ZAB with trypsin or heating at 100 degrees C for 30 min destroyed or reduced the antigenic activity respectively. Further purification of ZAB by filtration through Sephadex G-100 gave a preparation (ZAB2) which contained the common antigen as shown by the cross-reactivity of anti-ZAB2 rat serum with seven stains of N. gonorrhoeae. Fraction ZAB2 contained material which had a molecular weight less than 13,700 and was associated with the presence of material absorbing at 260 nm. The results of this study indicate that a low molecular weight antigen, which appears to be protein in nature and associated with nuclei acid, is common to the gonococcus and is the main antigenic component inducing reaginic (IgE) antibody in the rat.
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PMID:Induction of reaginic (IgE) gonococcal antibodies in the rat by a common antigen of Neisseria gonorrhoeae. 10 9

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

The role of human serum components in the phagocytosis of logarithmic-phase type 4 Neisseria gonorrhoeae by human polymorphononuclear leukocytes was investigated. The requirement of fresh normal human serum (FHS) for optimal phagocytosis and the fixation of human immunoglobulin (IgG) and complenet (C3) to the gonococcal cell surface suggested that both serum factors participate in the phagocytosis of these organisms. The percentage of neutrophils containing ingested organisms was directly proportional to the concentration of IgG purified from FHS. Absorption studies suggested that this natural IgG binds to a trypsin-sensitive surface protein on type 4 gonococci and cross-reacts with stationary-phase type 2 N. gonorrhoeae, group C Neisseria meningitidis, and Branhamella catarrhalis, but not with logarithmic-phase type 2 gonococci or other Neisseria species. Although complement alone did not promote phagocytosis, it enhanced IgG-mediated ingestion. Studies using C2-deficient serum or serum chelators indicated that the alternative complement pathway participates in this interaction.
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PMID:The role of natural IgG and complement in the phagocytosis of type 4 Neisseria gonorrhoeae by human polymorphonuclear leukocytes. 11 98

Pyocin inhibition of Neisseria gonorrhoeae and its feasibility as a gonococcal typing scheme were examined. Mitomycin C-induced pyocin lysates of Pseudomonas aeruginosa were able to selectively inhibit the growth of gonococcal strains. The particles associated with the inhibitory activity were non-dialyzable, heat labile, Pronase sensitive, trypsin resistant, and of large molecular weight by membrane and gel filtration techniques. The inhibitory activity was shown to be specific by absorption with sensitive and insensitive strains of N. gonorrhoeae and P. aeruginosa. Partial purification of pyocin lysates by ammonium sulfate precipitation followed by ultracentrifugation revealed phagelike particles consistent with high-molecular-weight R-type pyocines. These particles were associated with increased inhibitory activity and could be seen associated with the gonococcal cell surface. One hundred and six gonococcal strains could be differentiated on the basis of their sensitivity of 23 pyocin extracts. Thirty different patterns of pyocin inhibition were seen. Isolates from different body sites from the same patient could generally be identified as being similar strains. Strains isolated from known consorts had the same patterns. In general, agreement between pyocin typing and available epidemiological information was good.
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PMID:Pyocin sensitivity of Neisseria gonorrhoeae and its feasibility as an epidemiological tool. 40 41

Antigen was partially purified from Neisseria gonorrhoeae B370 saline wash and used to assay human sera for the presence of antibodies to N. gonorrhoeae. The antigen activity as monitored by counterimmunoelectrophoresis (CIE) is resistant to trypsin and papain but sensitive to heat and periodate oxidation. Of the sera from patients with bacteriologically confirmed cases of gonorrhea, 80% were positive by CIE using this antigen preparation. Of the sera in the negative control group 11% were reactive.
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PMID:Detection of antibodies to Neisseria gonorrhoeae by counterimmunoelectrophoresis. 41 47

Ribosomal preparations from Neisseria gonorrhoeae types 1 and 4 were examined for their in vitro stimulation of mouse splenocytes to determine the ribosomal moiety or contaminant responsible for the immunoproliferative activity. In immunodiffusion tests with homologous rabbit antiserum, crude 70S ribosomes formed four precipitin bands while the purified 30S and 50S subunits showed one major line. The same antiserum reacted with lysed N. gonorrhoeae and Neisseria meningitidis A cells but no precipitation occurred with Escherichia coli cells purified N. gonorrhoeae lipopolysaccharide (LPS). No membrane or LPS contaminant was detected in the purified 30S and 50S preparations. All the ribosomal preparations from virulent and non-virulent N. gonorrhoeae consistently stimulated the murine splenocytes. The mitogenic activity of the 30S and 50S ribosomal preparation was destroyed by treatment with trypsin but only slightly decreased by ribonuclease. It is suggested that the lymphoproliferative response elicited by gonococcal ribosomes is triggered by the protein moiety of the 30S or 50S subunits.
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PMID:Characterization of the mitogenic activity elicited by Neisseria gonorrhoeae ribosomal fractions. 41 60

Seventeen apparently unrelated isolates of Neisseria gonorrhoeae out of 2,123 tested produced a diffusible growth-inhibitory substance against other gonococci. The inhibitor was destroyed by trypsin, not blocked by bovine serum albumin, and not soluble in chloroform-methanol; each isolate was resistant to the inhibitor it produced. Thus, the substance differs from previously described gonococcal inhibitors, and since it fits the description of a bacteriocin we designated it gonocin. The use of gonocin for typing was complicated by the observation that susceptibility to gonocin appears to depend on the gonococcal colony type.
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PMID:Bacteriocin production by Neisseria gonorrhoeae. 82 28

A slide co-agglutination test (Phadebact Gonococcus Test) for the serological identification of Neisseria gonorrhoeae was assessed on gonococcal-like, oxidase positive colonies from 120 cultures, originating from about 6,500 consecutive tonsillo-pharyngeal specimens received at the Neisseria Department, Statens Seruminstitut. The test was performed after subculture on a serum-free medium, since this procedure was found to reduce the number of strains showing inconclusive reactions (pseudo co-agglutination). If this pseudo co-agglutination does occur, however, the test can be repeated with the addition of trypsin to the test system. This causes the previously inconclusive reactions to be reverted to clearly positive reactions in the case of gonococci, and to clearly negative reactions in more than half of the previously inconclusive reactions with other bacterial strains. The results obtained by the Phadebact Gonococcus Test were compared with those obtained by bacteriological identification procedures. Fifty-six of the 120 cultures examined contained gonococci, and all strains were identified by the slide co-agglutination test (five strains with the addition of trypsin). The remaining 64 cultures were negative or exhibited consistently pseudo co-agglutination (eight strains). The specificity and sensitivity of the reagent was further confirmed by the examination of 53 strains of Neisseria gonorrhoeae and 50 strains representing Neisseria species commonly occurring in tonsillo-pharyngeal specimens. The Phadebact Gonococcus Test was considered to be a reliable alternative to routine bacteriological identification of Neisseria gonorrhoeae.
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PMID:Identification of Neisseria gonorrhoeae in cultures from tonsillo-pharyngeal specimens by means of a slide co-agglutination test (Phadebact Gonococcus Test). 82 7


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