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)

Myofibrils from bovine longissimus muscle were obtained at 2 h postmortem and incubated in .10 to .35 M ionic strength buffers under various conditions in vitro. Increasing ionic strength or increasing the incubation time from 1 to 72 h decreased the turbidity of suspensions of myofibrils and increased myofibrillar solubilization (P less than .01 for both measures). The use of KCl or NaCl to elevate ionic strength gave essentially identical results, but lactate generally was ineffective in changing either the percentage myofibrillar solubilization or the turbidity of suspensions of myofibrils. Gel electrophoresis under denaturing conditions indicated that KCl was more effective than NaCl in causing the release of C-protein from myofibrils, and both salts were quite effective in dissociating M-protein, actin, troponin-T, tropomyosin, myosin light chain-3 and a 30,000-dalton molecular weight protein from myofilaments. Small increases in alpha-actinin also were observed, especially in samples incubated for 72 h. Substantially more myosin light chain-3, tropomyosin (or paratropomyosin) and troponin-T, and less actin and the 30,000-dalton protein, were released in samples incubated at pH 5.5 than at pH 7.0 (P less than .05). Electron micrographs indicated loss of thick filament ultrastructure after incubation for 24 h in either .1 or .3 M ionic strength, but the Z-lines were largely unaffected. In samples that had first been incubated with trypsin for 10 min, the Z-lines were virtually indistinguishable at .1 M ionic strength, and absolutely no myofibrillar structures could be discerned in samples incubated in .3 M ionic strength buffer.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Ionic strength and myofibrillar protein solubilization. 362 3

In radiobinding tests many group A, C and G streptococci react with IgG and IgA, irrespective of the antigen-combining sites, as well as with various other serum proteins, e.g. human serum albumin (HSA). The present study demonstrated that glutaraldehyde-aggregated, radiolabelled HSA (a*HSA), in comparison to monomeric HSA, binds more avidly to streptococci. Of group A streptococci, strains representing types M6, M12, M18, M46, M55 and M57 displayed pronounced binding of a*HSA whereas a number of other serotypes were non-reactive. The streptococcal sites involved proved to be relatively heat-resistant and highly sensitive to trypsin treatment. Human fibrinogen counteracted the binding of a*HSA. The uptake by M12 was inhibited strongly by rabbit antiserum raised against M12, whereas other antisera were less active. The results suggest that the bacterial structure binding a*HSA is a protein and that, in at least one serotype, M12, the binding occurs to the M-protein.
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PMID:Binding of aggregated human serum albumin to M12 and some other types of group A streptococci. 392 62

The production of M-protein antigen of Streptococcus equi was studied during in vitro growth in equine blood and in various media. Of 11 S equi strains studied, seven which had initially possessed 0.04 mg or less M-protein per 10 mg of streptococcal cell extract showed an increase in M-protein content after successive culture in heparinised horse blood. Maximum proliferation occurred in Todd-Hewitt (TH) medium with added 0.2 per cent w/v glucose when compared with TH medium alone or TH medium with 2 per cent w/v sucrose, starch, neopeptone or normal horse serum. The M-protein of these strains did not change after the addition of either neopeptone or normal horse serum to TH medium but declined with the addition of sugars. In experiments involving phagocytosis of S equi by equine polymorphs, the percentage of polymorphs which engulfed cocci was higher with a capsule-deficient strain (69.0 +/- 11.6 per cent) than with five typical encapsulated strains (21.1 +/- 7.0 per cent to 30.9 +/- 13.3 per cent). Phagocytosis of five typical strains was greater after growth in a trypsin-containing medium than in medium devoid of trypsin. Trypsin-grown cells took longer to kill mice than did normal cells. It was concluded that M-protein was one of the factors involved in the virulence of S equi.
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PMID:Production and biological properties of M-protein of Streptococcus equi. 400 57

The extraction of group A streptococcal antigens by group C phage-associated lysin has been confirmed. In addition to the T antigen the extract contained M-protein, group-specific polysaccharide and mucopeptide antigen which was difficult to remove. This method of extraction of the T antigen was compared with the trypsin method. The latter method was found to be of advantage in giving a pure specific antigen.
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PMID:Studies on two methods for extraction of streptococcal T antigens. 451 45

A new type of surface receptor for serum albumin was detected in strains of Streptococcus pyogenes (group A). This receptor, called type e, was different from albumin receptors in other streptococcal species. Only mouse and human serum albumin was bound to the receptor. The albumin-binding capacity was high: 2 X 10(8) bacterial organisms bound 11 micrograms of mouse albumin. The receptor was stable even when treated at 100 degrees C for 5 min. Binding of albumin was not mediated by lipoteichoic acid (LTA) because of lack of correlation to surface LTA, restricted albumin reactivity, and positive binding in presence of 2% Tween 20. Presence of albumin receptor type e correlated to presence of M-protein as measured by growth in the bactericidal test. All 51 M-protein positive group A streptococcal strains tested could bind mouse albumin whereas only 3 out of 8 M-protein negative strains showed positive binding (P less than 0.001). The sensitivity to trypsin digestion suggests that the albumin receptor is of protein nature or mediated by a protein.
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PMID:Demonstration of a receptor for mouse and human serum albumin in Streptococcus pyogenes. 632 28

Streptococcus pyogenes adheres to human epithelial cells in vitro and in vivo. To identify adhesins, cell wall components were extracted from S. pyogenes M6 with alkali or by treatment with mutanolysin and lysozyme. HEp-2 cells were incubated with extracts of S. pyogenes M6 and then analyzed by Western blot (immunoblot) assays, using antibodies to S. pyogenes. Only one streptococcal component (62 kDa) was bound to HEp-2 cells and was identified serologically as M6 protein. Experiments with pepsin-cleaved fragments of M protein indicated that the binding site was located at the N-terminal half of the molecule. M protein was bound selectively to two trypsin-sensitive surface components, 97 and 205 kDa, of HEp-2 cells on nitrocellulose blots of sodium dodecyl sulfate-polyacrylamide gels. Tritium-labeled lipoteichoic acid bound to different HEp-2 cell components, 34 and 35 kDa, in a parallel experiment, indicating that lipoteichoic acid was not complexed with M protein and does not mediate M-protein binding. The four HEp-2 components were unrelated to fibronectin since they did not react with specific antibodies. An M-protein-deficient (M-) strain of streptococcus (JRS75), grown in chemically defined medium, showed 73% less adhesion activity to HEp-2 monolayers than an M+ strain (JRS4). Streptococcal adhesion was insensitive to competitive inhibition by selected monosaccharides. These results indicate that M protein binds directly to certain HEp-2 cell membrane components and mediates streptococcal adhesion.
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PMID:M protein mediates streptococcal adhesion to HEp-2 cells. 830 Feb 5


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