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)

Pronase, trypsin and delta-chymotrypsin deplete rat alveolar peritoneal macrophages of EA (IgG)-binding activity. Trypsin and delta-chymotrypsin show an initially--under certain conditions and lasting--enhancement of receptor activity. Cycloheximide, an inhibitor of protein biosynthesis, accelerated the loss of Fc-receptors and inhibited their reappearance. There are differences between alveolar and peritoneal macrophages in the rate of loss as well as of regeneration of Fc-receptors.
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PMID:Effect of proteinases on EA (IgG)-binding receptors of rat macrophages. 39 42

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

An auxotroph of Bacillus subtilis 168 unable to synthesize D-alanine loses the ability to support endogenously energized transport when deprived of D-alanine. Revertants of the mutant retain transport activity. The loss of transport is specific for substrates taken up by active transport; substrates taken up by group translocation are transported at normal rates. The loss of transport can be retarded by pretreatment of the cells with inhibitors of protein synthesis. Since the loss of transport could be due to an alteration in a D-alanine-containing polymer, we investigated the incorporation of D-[14C]alanine into macromolecules. The major D-alanine-containing polymers in B. subtilis are peptidoglycan and teichoic acid, with 4 to 6% of the D-[14C]alanine label found in trypsin-soluble material. Whereas the peptidoglycan and teichoic acid undergo turnover, the trypsin-soluble material does not. Treatment of the trypsin-soluble material with Pronase releases free D-alanine. Analysis of acid-hydrolyzed trypsin-soluble material indicated that approximately 75% of the radioactivity is present as D-alanine, with the remainder present as L-alanine. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of partially purified D-[14C]alanine-labeled membranes indicated the presence of two peaks of radioactivity (molecular weights, 230,000 and 80,000) that could be digested by trypsin. The results suggest that D-alanine may be covalently bound to cellular proteins.
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PMID:D-alanine incorporation into macromolecules and effects of D-alanine deprivation on active transport in Bacillus subtilis. 41 65

1. Aqueous extracts of digestive glands of specimens of the dorid nudibranchs Cadlina flavomaculata, Doriopsilla albopunctata, Anisodoris nobilis, Archidoris montereyenis, and A. odhneri were lethal when injected into shore crabs and when injected intraperitoneally into mice. 2. Aqueous extracts of the degestive glands of Doriopsilla albopunctata and of Anisodoris nobilis were shown by bioassay (guinea pig ileum)and by chemical determination to contain histamine. The amount present was far too small to account for the toxicity of the glands. 3. Extracts of the digestive glands of Anisodoris nobilis were fractionated by column chromatography on Biogel P-2 to yield an active fraction designated "dorid toxin". This produces lethargy and bradycardia in mice. In anesthetized rats it produces sustained (60 min or more) bradycardia and hypotension. On isolated hearts, especially spontaneously beating guinea pig atria, it has negative inotropic and chronotropic effects. 4. Dorid toxin has a molecular weight under 8000. It is heat stable and is not destroyed by trypsin, chymotrypsin or Pronase. It is therefore unlikely that it is a polypeptide.
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PMID:Toxicity and pharmacology of extracts from dorid nudibranches. 45

Bacteriocin-like substances were commonly produced by slow-growing Rhizobium japonicum and cowpea rhizobia on an L-arabinose medium. Antagonism between strains of R. japonicum was not detected in vitro; however, such strains were often sensitive to some bacteriocins produced by cowpea rhizobia. Inhibitory zones (2 to 8 mm from colony margins), produced by 58 of 66 R. japonicum test strains, were reproducibly detected with Corynebacterium nebraskense as an indicator. Quantitative production was not related to symbiotic properties of effective strains, since nine noninfective strains and one ineffective strain produced bacteriocin. Eight R. japonicum strains that did not produce bacteriocin nevertheless formed effective nodules on soybeans. R. japonicum strains that produced bacteriocin in vitro had no antagonistic effect on nonproducer strains during soybean nodulation. Under controlled conditions, a nonproducer (3I1b135) predominated over a bacteriocin producer (3I1b6) when inoculated at 1:1 and 1:9 ratios. Depending on the particular ratio, up to 38% of the total nodules formed were infected with mixed combinations. The bacteriocin(s) had a restricted host range and antibiotic-like properties which included the ability to be dialyzed and resistance to heat (75 to 80 degrees C, 30 min), Pronase, proteinase K, trypsin, ribonuclease, and deoxyribonuclease. R. japonicum strains representing genetic, serological, cultural, and geographic diversity were differentiated into three groups on the basis of bacteriocin production.
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PMID:Bacteriocin-like substances produced by Rhizobium japonicum and other slow-growing rhizobia. 57 16

Three different extracts of Thermoactinomyces sacchari were analyzed for their antigenicity and physical-chemical properties. Rabbit antiserum to each preparation, tested by immunodiffusion in gel, demonstrated that the most potent immunogen was that prepared by the double-dialysis method. This extract also contained the greatest number of precipitating antigens as detected by gel filtration. All extracts, analyzed by column chromatography on Sephadex G-75, were heterogeneous in that they contained large- and small-molecular-weight fractions. Precipitins in each extract were detected in column eluates of relatively low ultraviolet absorption and were of a similar molecular size range. Chemical analysis of purified antigens demonstrated protein and carbohydrate. The culture supernatant contained the greatest amount of carbohydrate (66%), and the soluble extract of bacterial cells contained the greatest amount of protein (68%). Several antigens were partially sensitive to the proteolytic enzymes Pronase and trypsin, but none was sensitive to lysozyme. These results demonstrate that there are multiple-antigen systems in T. sacchari and that, of the samples analyzed, the double-dialysis method of antigen preparation yields the most potent antigens.
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PMID:Characterization of Thermoactinomyces sacchari antigens. 66 9

The partially purified glucosyltransferase (GTF) fraction synthesizing primarily water-insoluble glucans, GTF-A, and the homogeneous fraction synthesizing water-soluble glucans, GTF-B, were utilized to assess the binding of GTF activity to the cell surface of Streptococcus mutans GS-5. Growth of the cells in either Todd-Hewitt broth or a chemically defined medium did not appear to affect the ability of the cells to bind either enzyme fraction. Heat inactivation of the cells did not singificantly reduce the interaction of the enzymes with the cells. Cell surface glucan molecules appear to be involved in GTF binding to the cells because: (i) dextranase or alpha-1,3-glucanase treatment of the cells markedly reduced enzyme binding; (ii) the inclusion of soluble dextrans in the binding assays reduced both GTF-A and GTF-B binding to the cells; and (iii) pretreatment of the cells or the GTF-B fraction with soluble dextrans before binding significantly reduced enzyme binding to the cells. In addition, enzyme binding appears to require a cell surface protein component because Pronase, but not trypsin, treatment of cells reduced enzyme binding. Furthermore, the removal of a portion of the cell surface GTF-glucan complex with 3 N NaCl appears to provide additional binding sites for the enzymes. These results are interpreted in terms of the mechanism of the conversion of extracellular GTF to the cell-associated form.
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PMID:Interaction of glucosyltransferase with the cell surface of Streptococcus mutans. 66 17

Human albumin prepared by the trichloroacetic acid method was treated with bromelin, ficin, papain, pronase or trypsin. Pronase- or trypsin-treated albumin showed four fragments on polyacrylamide disc electrophoresis. When rabbit antiserum to pronase-treated albumin was adsorbed with monkey albumin, antibody with human specificity was completely abolished, whereas anti-albumin serum adsorbed with pronase-treated albumin retained the antibody to human albumin. It was considered that antigenic site with human specificity in albumin structure was inactivated by pronase.
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PMID:Fragmentation of human albumin with proteolytic enzymes and its antigenicity with special reference to human-specificity. 69 18

Polyacrylamide gel electrophoretic analysis and immunoprecipitation were used to study glycoproteins from purified Rauscher murine leukemia virus (R-MuLV) and from AKR thymic lymphoblastoid cell membranes. In addition to gp70, a minor glycoprotein of approximately 52,000 daltons (gp52) was demonstrated in purified R-MuLV preparations, which was antigenically related to gp70. Analysis of R-MuLV glycopeptides obtained after exhaustive Pronase digestion showed that gp70 has at least two different glycopeptide size classes with molecular weights of 5,100 and 2,900, respectively. gp52, however, contained only a single glycopeptide size class of approximately 5,100 daltons, indicating that the two glycoproteins contain distinct carbohydrate components. Trypsin treatment of R-MuLV converted gp70 into a product with a molecular mass of approximately 52,000 daltons as well as a 45,000-dalton minor product, with little effect on virus infectivity. Similarly, trypsin treatment of 125I-labeled glycoproteins derived from AKR mouse lymphoblastoid cell membranes generated fragments antigenically related to gp70 and similar in size to those obtained by trypsin treatment of R-MuLV. In both cases, the appearance of cleavage products was accompanied by a decrease in gp70 during trypsin treatment. The occurrence of glycosylated components antigenically related to gp70 in AKR membrane glycoprotein preparations and in purified R-MuLV preparations which were similar to those generated by trypsin treatment supports the concept that these minor components arise from proteolytic cleavage of gp70.
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PMID:Origin of the minor glycoproteins of murine leukemia viruses. 70 58

A substance inhibitory to protein synthesis was purified from mouse skeletal muscle by gel filtration and ion-exchange chromatography, as well as by centrifugation on sucrose gradients. The molecular weight of the inhibitor, determined by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, was 71000. The inhibitory activity was insensitive to ribonuclease A, deoxyribonuclease I and phospholipase C. It was sensitive to Pronase treatment but insensitive to heat-treatment and trypsin degradation. The present results, taken together with previous studies, indicate that the site of action of the inhibitor is not on the initiation phase of protein synthesis but rather at a step after the binding of aminoacyl-tRNA to ribosomes. The increased inhibitor activity found in dystrophic muscle is discussed.
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PMID:Studies of a factor from dystrophic mouse muscle inhibitory towards protein synthesis. 74 60


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