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)

Escherichia coli ompA mutants are tolerant to colicin L-JF246. This tolerance can be overcome by a variety of treatments that have as their target the outer membrane or the peptidoglycan layers of the cell envelope. Thus, increasing the concentration of colicin L, releasing lipopolysaccharide from the outer membrane by treatment of intact cells with ethylenediaminetetracetic acid (EDTA), converting cells to spheroplasts by treatment with lysozyme-EDTA or penicillin, or trypsin, treatment of intact cells will result in an increased colicin sensitivity. These treatments alter the outer membrane of ompA mutants and suggest that the altered outer membrane may allow the penetration of at least a portion of the colicin L molecule to a site of action located within this barrier. To substantiate this, we have demonstrated that membrane vesicles prepared from ompA mutants are sensitive to colicin L and that 14C-labeled colicin L binds rapidly to both the outer and inner membrane fractions of the cell.
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PMID:Defeat of colicin tolerance in Escherichia coli ompA mutants: evidence for interaction between colicin L-JF246 and the cytoplasmic membrane. 41 31

An extracellular protein-polysaccharide-lipide (PPL) complex from exponentially growing cultures of Myxococcus virescens was purified by phosphate precipitation and gel chromatography. The high molecular weight slime polymer appeared homogenous upon isoelectric focusing. The PPL complex exhibited proteolytic activity against gelatin and the activity was only partly reduced by heat treatment. The function of the slime polymer as protein denatured was studied. The complex formed micelles similar to anionic detergents and it inhibited the precipitation and coagulation of proteins by trichloroacetic acid. Lysozyme was totally inactivated when treated with the PPL complex. By gel chromatography binding studies, the PPL complex was found to bind lysozyme in the ratio of 1 to 5.8 (w/w). After separation of added protein from the complex the anticoagulation effect on the protein remained. The biological function of the PPL complex was demonstrated with hemoglobin. When all susceptible peptide bonds in PPL-treated hemoglobin were hydrolyzed by trypsin only 20% in the urea-denatured protein were attacked. The combined role of slime and proteolytic activity is discussed.
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PMID:Myxobacterial slime and proteolytic activity. 41 87

During purification of E2R using oligo(dT)-cellulose chromatography, a receptor accessory factor (RAF) was identified in the cytosol of mouse kidney. This factor stimulates the binding of purified E2R to oligo(dT)-, oligo(dC)-, and oligo(dA)-cellulose as well as to DNA cellulose. It is a heat-stable, trypsin-resistant protein with an apparent molecular weight of between 10 and 30,000 daltons. Although structurally unrelated, similar stimulation of oligonucleotide binding was seen with calf thymus histones and, to a lesser extent, egg white lysozyme. Individual histones, especially H2a, H2B, and H3, also facilitate rebinding of purified E2R to oligo(dT)-cellulose, while H1 is less effective. Furthermore, histones stabilize the holoreceptor during sedimentation at 4 degrees and 12 degrees C. The N- and C-terminal half molecules of H2b were generated by cyanogen bromide-mediated cleavage and the N-terminal half was found to duplicate the effects of the parent molecule, both in binding and holoreceptor stabilization. These data suggest that the in vivo binding of E2R to DNA can be modulated by accessory proteins of cytosol and nuclear origin.
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PMID:Stimulation of oligonucleotide binding of estradiol receptor complexes by accessory proteins. 49 27

The binding isotherms of native bovine serum albumin with cationic detergents, such as octyl, decyl, dodecyl and tetradecylpyridinium bromides were determined at pH 6.8 and 3.4 at 25 degrees C. The isotherms for dodecyl and tetradecylpyridinium bromides were also determined at 3 degrees C. The average number of detergent cations bound increased with increasing hydrocarbon chain length. At low detergent concentration the binding of all alkylpyridinium bromides was smaller at pH 3.4 than at pH 6.8. Dodecylpyridinium bromide was bound to native beta-lactoglobulin, aldolase, ovalbumin, haemoglobin, myoglobin, lysozyme, trypsin and ribonuclease at pH 6.8. No binding occurred to alpha-chymotrypsin and chymotrypsinogen. The free enthalpy change, --delta G degrees, calculated from intrinsic association constants K was determined.
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PMID:Protein-cationic detergent interaction. Equilibrium dialysis study of the interaction of bovine serum albumin and other proteins with alkylpyridinium bromide. 49 43

Fourier transform infrared and laser Raman spectroscopies were used to study the effects of dodecylpyridinium bromide on the conformation of haemoglobin, myoglobin, bovine serum albumin, ribonuclease, ovalbumin, lysozyme, trypsin and beta-lactoglobulin in aqueous solution. Addition of the cationic detergent caused a decrease in alpha-helix conformation in highly helical proteins. At low detergent concentrations stabilization of beta-sheet conformation was observed.
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PMID:Protein-cationic detergent interaction. Fourier transform infrared and laser Raman spectroscopic studies on the interaction between proteins and dodecylpyridinium bromide. 49 44

Four bacteriocins of L. fermenti, 3 bacteriocins of L. brevis and 1 bacteriocin of L. buchneri were studied with respect to morphology of the inhibition growth zones of the indicator strains, capacity for diffusion through cellophane, sensitivity to high temperature, bacterial proteases, trypsin, chymotrypsin, pepsin, papain, nucleases and lysozyme. According to the differences in their properties the bacteriocins were classified as belonging to 8 types, including 4 types of L. fermenti bacteriocins and 3 types of L. brevis bacteriocins.
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PMID:[Bacteriocin properties of Lactobacillus fermenti, Lactobacillus brevis and Lactobacillus buchneri]. 50 77

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 translation of ovomucoid mRNA in a reticulocyte lysate protein-synthesizing system yields a precursor form which contains an NH2-terminal extension of 23 amino acid residues. Edman degradation of radioactive translation products (pre-ovomucoid) identified the following sequence: formula : (see text), where the initiator methionine (in parentheses) is the only residue cleaved from the NH2 terminus during cell-free synthesis and the vertical line indicates the site at which pre-ovomucoid is cleaved in vivo to yield ovomucoid. The precursor sequence differs from those of two other proteins (pre-lysozyme and pre-conalbumin) secreted by the same cell, but resembles these and other secretory protein "signal peptides" in both length and hydrophobicity. Pre-ovomucoid does not interact with trypsin in the same manner as mature ovomucoid.
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PMID:Precursor of egg white ovomucoid. Amino acid sequence of an NH2-terminal extension. 72 26

The peptide map obtained by tryptic hydrolysis of the lysozyme oxidized at the S--S-bonds was characterized and compared with that of tryptic hydrolysis of the reduced lysozyme. It was shown that the mobility of peptides containing oxidized amino acid residues is decreased under electrophoresis and chromatographic treatment. Under a decrease in the peptide charge during oxidation, the changes in electrophoretic and chromatographic mobilities show a correlation. In case when the peptide charge remains unchanged, only chromatographic mobility may be altered. It is demonstrated that the cystein residues significantly interfere with the effects of trypsin on the adjacent bonds.
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PMID:[Mobility on peptide maps of peptides obtained by tryptic hydrolysis of lysozyme oxidized at the S-S-bonds]. 73 12

The resistance of native and trypsin-treated [14C] glucose-labeled cell walls to degradation by lysozyme and human lysosomal enzymes was confirmed. In contrast, chemically N-acetylated cell walls undergo significant degradation by these enzymes in the pH range of 4.5 to 5.5 without prior removal of the group-specific carbohydrate. N-acetylation after removal of the group A carbohydrate by formamide extraction renders the cell walls considerably more susceptible to these enzymes than by formamaide extraction alone. It appears, therefore, that unless N-acetylation can occur in vivo, streptococcal cell walls are minimally degraded, if at all, by human peripheral blood leukocytes or lysozyme. Examination of leukocyte extracts from normal subjects and patients with post-streptococcal syndromes revealed no qualitative differences in ability to dissolve streptococcal cell walls.
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PMID:Degradation of 14C-labeled streptococcal cell walls by egg white lysozyme and lysosomal enzymes. 77 36


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