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)

Using an assay of macrophage migration, where the cells emigrate from an agarose droplet, it was found that the neutral proteases trypsin, chymotrypsin, Pronase and elastase have MIF-like activity. Appropriate enzyme inhibitors counteract this effect. To twelve synovial fluids from patients with inflammatory arthritis, which have MIF-like activity (migration index between 0-3 and 0-7) protease indhibitors (Trasylol, ovomucoid and soybean inhibitor) were added. Ten of the fluids lost some of their MIF-like activity with at least one inhibitor. Phenylmethylsulphonylfluoride counteracted totally the MIF-like activity of the two fluids tested. It is concluded that MIF-like activity of inflammatory synovial fluids is due, at least partially, to proteases.
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PMID:Migration inhibition factor-like activity in inflammatory synovial fluids might be due to proteases. 79 49

A strain-specific virulence-associated antigen has been found in Neisseria gonorrhoeae strain F-62. Using immunodiffusion in agar gel, it has been shown that the antigen is distinguishable from endotoxin and the virulence-associated toxic protein. It does not appear to be derived from pili. The antigen was not detected in T1 and/or T2 colony type cultures of 10 other isolates. It exhibited a possible partial immunological relationship with an antigen found in one additional strain. It was susceptible to digestion with Pronase and trypsin.
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PMID:Strain-specific virulence-associated antigen of Neisseria gonorrhoeae. 80 45

A new, simple method has been developed for the purification of Streptomyces griseus trypsin [EC 3.4.21.4] from Pronase. Only a single operation of affinity chromatography on an agarose derivative, which was easily prepared by coupling a tryptic digest of salmine to cyanogen bromide-activated Sepharose 4B, was required. A high degree of homogeneity was demonstrated for the purified enzyme by disc electrophoresis, SDS-polyacrylamide gel electrophoresis and gel filtration, as well as by active-site titration. The behavior of a carboxypeptides B [EC 3.4.12.3]-like enzyme present in Pronase is also discussed.
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PMID:Affinity chromatography of trypsin and related enzymes. III. Purification of Streptomyces griseus trypsin using an affinity adsorbent containing a tryptic digest of protamine as a ligand. 81 28

The topography of the external surface of the human red cell membrane has been studied using an impermeant radioactive probe, [125I]diazodiiodosulfanilic acid, which binds covalently to protein groups of the membrane following reaction with intact cells. The pattern of labeling was assessed by sodium dodecyl sulfate-polyacrylamide disc gel electrophoresis followed by sequential analysis of single gels for carbohydrates (by staining with the periodic acid-Schiff (PAS) reagent), for proteins (by staining with Coomassie blue), and for radioactivity (by counting gels sliced in 2-mm segments). The radioactive probe bound to membrane polypeptides with apparent molecular weights of 94,200, 58,100, and 46,500 (Peaks A, B, and C, respectively). Peak A co-migrated with a small periodic acid-Schiff-positive band and protein Band 3 (nomenclature of Steck) (Steck, T.L. (1974)J. Cell Biol. 62: 1-19). Peak B migrated with protein Band(s) 4.5 slightly ahead of the major membrane glycoprotein (PAS-1). Peak C migrated like glycoprotein PAS-2 and protein Band 5, the actin-like, water-soluble membrane protein. In contrast to lactoperoxidase iodination and a number of other probes, [125I]diazodiiodosulfanilic acid reacted minimally with the major membrane glycoprotein, glycophorin. When it was reacted with isolated ghosts, all molecular weight classes of polypeptides were labeled. Treatment of labeled cells with neuraminidase or trypsin altered the glycoprotein staining pattern, but not the radioactive peaks. On the other hand, Pronase eliminated the Mr=94,200 radioactive peak, diminished the other two radioactive peaks, and profoundly changed the glycoprotein and protein staining patterns. Treatment of the membranes of labeled cells in a low ionic strength alkaline medium did not alter radioactive peaks and demonstrated that Peak C differed from the actin-like membrane protein. A nonionic detergent, Triton X-100, solubilized all radioactive components. The studies have defined the binding of [125I]diazodiiodosulfanilic acid to external proteins of the human red cell membrane. Its pattern of reaction differs quantitatively and qualitatively from other commonly used reagents, and it provides a useful additional vectorial probe for the study of membrane topography. Its reactions provide further evidence of the organizational complexity of the red cell membrane and emphasize the fact that interpretation of information derived from the use of membrane probes must take into account the differences resulting from the properties of the probing reagents themselves.
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PMID:Topography of the external surface of the human red blood cell membrane studied with a nonpenetrating label, [125I]diazodiiodosulfanilic acid. 83 50

Purified gp71 of Friend murine leukemia virus (FLV) can interfere with virus infection, absorb neutralizing antibody, and in the presence of group-specific anti-gp71 antibody, hemagglutinate sheep erythrocytes. Interference by FLV gp71 with several murine leukemia viruses (MuLV) was tested in the XC and S + L- assay systems. Treatment of gp71 with trypsin or Pronase eliminated its interfering capacity. However, treatment with neuraminidase or a mixture of glycosidase enzymes, which left the major serological properties of gp71 intact, did not reduce the interference potential of gp71 for FLV or AKR MuLV. The capacity of gp71 to absorb type- or group-specific virus-neutralizing antibodies was similarly affected by the various enzyme treatments. In contrast, indirect hemagglutination by gp71 was abolished not only by proteases but also by treatment with glycosidase enzymes, although neuraminidase had no effect. Preliminary data indicate that infectivity of FLV or xenotropic MuLV was not affected by short treatment with glycosidase enzymes.
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PMID:Role of carbohydrate in biological functions of Friend murine leukemia virus gp71. 83 28

Several human fecal isolates of Bacteroides have been found to produce bacteriocins. The bacteriocin-producing strain T1-1 was studied in the most detail. Strain T1-1 belongs to the 0061-1 deoxyribonucleic acid (DNA) homology group of Bacteroides. This homology group phenotypically resembles Bacteroides thetaiotaomicron but has little DNA homology with it. The bacteriocin-producing strains T1-12 and T1-48 belong to the 3452-A DNA homology group. This group has DNA homology with B. thetaiotaomicron and Bacteroides ovatus. The bacteriocin-producing strain T1-42 remains unidentified in that it does not belong to any recognized DNA homology group of the saccharolytic intestinal bacteroides. The extracellular bacteriocin produced by strain T1-1 was specifically bactericidal for other bacteria within the genus Bacteroides. The highest bacteriocin titers (32 to 64) were produced in complex media, with only trace amounts being produced in a defined medium. The bacteriocin appeared to have a high molecular weight (>/=300,000) and was unusual because it was stable from pH 1 to 12 and only a 50% reduction in activity resulted after 15 min at 121 degrees C in an autoclave. It was inactivated by trypsin and Pronase. Strain T1-1 was isolated from all three fecal samples obtained over a 25-week period from an individual who was part of a National Aeronautics and Space Administration mock Skylab flight. Strains T1-12, T1-48, and T1-42 were isolated only from the first fecal sample. Each of these strains was immune to the bacteriocins produced by the others. These strains were found to coexist in the colon with a larger population of non-bacteriocin-producing, bacteriocin-susceptible strains of Bacteroides.
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PMID:Bacteriocin production by strains of Bacteroides isolated from human feces and the role of these strains in the bacterial ecology of the colon. 85 24

A glycoprotein of mol.wt. 2x10(6) was isolated in homogeneous form from pig gastric mucus by isopycnic centrifugation in CsCl but without enzymic digestion or reductive cleavage of disulphide bonds. Digestion of the purified glycoprotein with trypsin, pepsin or Pronase resulted in the formation of glycoprotein subunits, of mol.wt. 5.2x10(5)-5.8x10(5), one-quarter that of the undigested glycoprotein. The glycoprotein subunits were isolated by gel filtration and shown to contain all the carbohydrate present in the undigested glycoprotein, but 18.6-25.6% of the total amino acids originally present were lost on digestion. The relative amount of threonine, serine and proline had increased from 41% (w/w) in the undigested glycoprotein to 61-67% of the total amino acids in the glycoprotein subunits after digestion. The results support the previously proposed structure for the glycoprotein, namely that of four subunits joined by disulphide bridges. These results show the presence of two distinct regions in the glycoprotein molecule, one rich in threonine, serine and proline, which is glycosylated and resistant to proteolyis, whereas the other, with an amino acid composition more characteristic of a globular protein, is not glycosylated and is susceptible to proteolysis. In addition, the region that is susceptible to proteolysis contains the disulphide bridges which join the glycoprotein subunits together to form the gastric glycoprotein.
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PMID:The action of proteolytic enzymes on the glycoprotein from pig gastric mucus. 86 29

1. The properties of rat liver cytoplasmic alpha-tocopherol binding protein have been studied. 2. The binding protein sedimented in the 3 S region of sucrose density gradients, and gel filtration indicated an approximate molecular weight of 30 500. 3. Of the tissues examined by the present assay, binding was detectable only in the liver. 4. Optimal binding was achieved by incubation at 26 degrees C for 4 h and was independent of pH between 7.4 and 9.0. 5. Pronase completely abolished binding. The binding protein was, however, almost completely resistant to trypsin, and unaffected by RNAase, DNAase, triacylglycerol lipase, and phospholipase C. 6. A variety of tocopherol analogues and other lipid-soluble compounds were tested for their ability to compete for binding. Only alpha-tocopherol and to a lesser extent alpha-tocotrienol and gamma-tocopherol exhibited competition. alpha-Tocopherol acetate, alpha-tocopherol quinone and 6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid had no effect on binding. 7. Tocopherol binding was reversible, and the tocopherol was not metabolized during incubation.
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PMID:Rat liver alpha-tocopherol binding protein. 87 71

Previous data from this laboratory showed that certain phage group 2 staphylococci contain a large 56S virulence plasmid containing genes that code for both exfoliative toxin (ET) and a specific staphylococcin. Optimal cultural conditions for bacteriocin production were similar to those found for ET production. The bacteriocin is an extracellular product produced in small quantities that can be neither extracted from cell pellets with 1 M NaCl nor induced with mitomycin C. The staphylococcin is active against a wide variety of gram-positive organisms and also against group 2 staphylococcal strains that have been cured of the plasmid carrying the staphylococcin marker. The bacteriocin is not inactivated by oxidation, mechanical agitation, or boiling for 15 min. It is sensitive to the action of trypsin and Pronase but not lysostaphin and is stable within a pH range of 4 to 9. It has an isoelectric point of approximately 7.7. Removal of the ampholytes and glycerol from electrofocused staphylococcin preparations resulted in total loss of bacteriocin activity.
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PMID:Production and properties of a staphylococcin genetically controlled by the staphylococcal plasmid for exfoliative toxin synthesis. 87 Apr 29

1. A new method for the assay of insect prothoracicotropic hormone (PTTH) is described, using fourth instar larvae of Manduca sexta. Larvae neck-ligated at a critical time to prevent release of PTTH from the head fail to undergo the next larval moult. Such ligated larvae moult to fifth instar larvae or larval-pupal intermediates after injection of brain homogenates from Manduca larvae, pupae or pharate adults. The degree of response is proportional to the concentration of brain homogenate injected. 2. The source of PTTH in the pupal brain is the dorsal region of the protocerebrum containing the lateral neurosecretory cells. Microhomogennates of single pieces of brain showed activity with this method. 3. PTTH activity in partially purified extracts is water soluable, stable to boiling for 10 min, and is destroyed by Pronase or trypsin.
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PMID:Prothoracicotropic hormone in Manduca sexta: localization by a larval assay. 87 Jun 1


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