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)

Extracts of the marine polychaetous annelid, Amphitrite ornata, agglutinate rat, rabbit, chicken and human erythrocytes and in other work have been shown to inhibit the growth of Ehrlich ascites tumors in mice. Fractionation of extracts on Sephadex G-100 gave three active fractions with molecular weights of 30 000, 54 000 and 100 000. The 30 000 dalton fraction (B) was purified 72-fold by ammonium sulfate precipitation, gel filtration and preparative disc gel electrophoresis. The purified hemagglutinin, amphitritin, was homogenous on analytical disc gel electrophoresis at four different pH values and gave a sharp boundary in sedimentation velocity ultracentrifugation. The three fractions showed paralled specificity toward rat and chicken erythrocytes, the former giving the higher titer. The purified agglutinin was active toward human blood groups A, B and O and exhibited 4-fold higher activity toward group A. The hemagglutinin titer against rat red blood cells was lowered only by N-acetylgalactosamine, the terminal sugar residue of the group A determinant. None of the saccharides tested inhibited agglutination of chicken erythrocytes. Hemagglutinin activity was insensitive to dialysis or treatment with EDTA. The activity was not affected by digestion with trypsin or pronase, but was destroyed by phenol extraction. Analytical disc gel electrophoresis showed one protein band with high anodal mobility at pH 8.5, which was not affected by proteolytic enzymes but was removed by phenol. Activity was unaffected by heating at 70 degrees C for 30 min but was destroyed by similar treatemtn at 85 degrees C. Activity was at a maximum at pH 7-9 and decreased reversibly down to pH 4 at which point it was irreversibly inactivated. The higher molecular weight agglutinin (A1) could be dissociated to give amphitritin by treatment with 6M urea of precipitation in 55% (NH4)2SO4. This dissociation was not reversed by dialysis. Amphitritin is a glycoprotein with a molecular weight determined by gel filtration of 30 000 and by approach to equilibrium sedimentation of 32 000. Amino acid analysis showed a preponderance of aspartic and glutamic acids and relatively large amounts of glycine, proline, alanine, valine and cysteine. The carbohydrate moeity which represented 12.8% of the molecule, contained mannose, galactose, glucosamine and sialic acid. Amphitritin is the first hemagglutinin to be isolated from a polychaetous annelid.
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PMID:Isolation and characterization of a hemagglutinin from Amphitrite ornata, a polychaetous annelid. 0 17

Human, guinea pig and rabbit skin homogenates were digested with trypsin and extracted with phenol water. Antisera were raised in guinea pigs and rabbits by immunization with extract recovered from the water phase (TPW extract). All sera showed increased titres in indirect haemagglutination tests. The results of absorption and inhibition experiments indicated antibodies against a common antigenic determinant. These antibodies also agglutinated erythrocytes sensitized with autologous antigen. In addition, serum from rabbits immunized with human or guinea pig skin extract contained antibodies against species-specific determinants. Rabbit antiserum precipitated guinea pig skin extract. The antigen involved had specificity identical with that of an antigen in the human, but not in the rabbit skin, extract. Oxidation of the human TPW extract with periodate destroyed the precipitinogen and the species-specific haemagglutinogen while the common determinant was not affected.
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PMID:Specificity of antigens in aqueous phenol extracts of skin examined by means of guinea pig and rabbit immune sera. 5 Oct 11

Homogenated stratum coreum, callus and psoriatic scales were extracted with (1) phenol water (PW) and (2) the combined use of trypsin digestion and phenol water extraction (TPW). The serological properties of the various preparations obtained were compared, using indirect haemagglutination, absorption and inhibition tests. The PW and TPW water phases contained two different antigens which were common to all three tissues. In addition, the periodate-treated TPW water phase of stratum corneum contained an erythrocyte-sensitizing antigenic determinant. This, however, cross-reacted with the untreated and periodate-treated preparation of psoriatic scales, whereas callus lacked the determinant present after treatment with periodate. Apparently callus and psoriatic scales lacked some components present in stratum corneum, but determinants specific for callus or psoriatic scales were not detected.
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PMID:Comparison of human stratum corneum, callus and psoriatic scales by means of serological methods. 6 92

The pattern of development of antibody-forming cells in BALB/c mice after immunization with PW-LPS or TCA-LPS was shown to be different. On days 10 and 20, the primary response to PW-LPS was characterized by a low level of IgM synthesis. The plaque-forming cell (PFC) response to TCA-LPS, however, increased from day 10 to day 20. Initially, IgM was the only detectable antibody synthesized but by day 20 a significant number of IgG-producing spleen cells had developed. After a secondary immunization with the appropriate lipopolysaccharide (LPS) preparation, IgG-producing spleen cells were detected in mice immunized with either PW-or TCA-LPS. Partial removal of the LAP or TCA-LPS with phenol or trypsin and pronase significantly reduced the PFC response, suggesting that the protein moiety played an influential role in the immunogenicity of TCA-LPS. The TCA-LPS contained the same antigenic dterminants as PW-LPS, so any difference observed between PFC response was not due to any associated immunogenic moiety.
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PMID:Plaque-forming cell response in BALB/c mice to two preparations of LPS extracted from Salmonella enteritidis. 8 28

Group-specific and type-specific antigens have been identified and purified from sonic extracts of Capnocytophaga. The group-specific antigen, which was purified by affinity chromatography, was found to be identical to an antigen present in all 26 strains tested. The antigen is sensitive to trypsin, sodium dodecyl sulfate and heat labile, and composed predominantly (55%) of protein. The type-specific antigen, which was obtained by preparative immunoelectrophoresis, was found to be present in only 3 of the 26 strains tested. This antigen was resistant to heat, trypsin, and sodium dodecyl sulfate and was primarily composed of carbohydrate (47% phenol-sulfuric acid-positive material, 8% amino sugar). Agglutination and fluorescent antibody data suggest that both the group- and type-specific antigens reside on the cell surface.
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PMID:Group and type antigens of Capnocytophaga. 10 14

The properties of a (Na+ plus K+)-dependent ATPase (ATP phosphohydrolase, EC 3.6.1.3) activator contained in leukocytic extracts was investigated. Intact polymorphonuclear leukocytes release the activator in a time- and temperature-dependent process. It is non-dialyzable through cellophane; inactivated by protease, trypsin, or phenol; contains essential sulfhydryl groups; and is heat and acid labile. Treatment of ATPase with the activator and subsequent removable of the activator from mixtures did not reverse the ATPase activation.
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PMID:Activation of rabbit brain microsomal (Na+ plus K+)-dependent ATPase by a leukocytic product. 12 98

1. In addition to poly(ribitol phosphate) the walls of a bacteriophage-resistant mutant of Staphylococcus aureus H contain glycerol phosphate residues that are not removed on digestion with trypsin or extraction with phenol. 2. The glycerol phosphate is present in a chain, containing three or four glycerol phosphate residues, which is covalently attached to the peptidoglycan through a phosphodiester linkage to muramic acid; this linkage is readily hydrolysed by dilute alkali. 3. The degradative studies described suggest that the poly(ribitol phosphate) chains of the wall teichoic acid may be attached to the wall by linkage to this glycerol phosphate oligomer.
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PMID:Studies on the linkage between teichoic acid and peptidoglycan in a bacteriophage-resistant mutant of Staphylococcus aureus H. 12 54

Glycophorin A, the major human erythrocyte sialoglycoprotein, contains a significant amount of phosphorus when isolated by the lithium diiodosalicylate-phenol procedure. Only a small percentage (approximately 1%) of this phosphorus is phosphoprotein. 31P nuclear magnetic resonance (NMR) analysis of glycophorin A has identified the remaining phosphorus content as phospholipid in origin. From the 31P chemical shifts, the phospholipid has been identified as diphosphoinositide. 31P NMR spectra of the peptides produced by trypsin hydrolysis of glycophorin A reveal that all the diphosphoinositide is closely associated with the hydrophobic region of the protein, suggesting that there is a specific affinity between this phospholipid and the intramembranous portion of glycophorin A.
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PMID:31P nuclear magnetic resonance evidence for polyphosphoinositide associated with the hydrophobic segment of glycophorin A. 19 Oct 66

C3H/HeJ mice were used to study the origin and nature of endotoxin-induced glucocorticoid antagonizing factor (GAF). In conventional mice GAF is believed to be responsible for a variety of effects that occur as a result of an injection of endotoxin, including the inhibition of hormonal induction of hepatic phosphoenolpyruvate carboxykinase and of glyconeogenesis. Responses in such animals are seen whether the endotoxin is extracted with phenol-water or with trichloroacetic acid. C3H/HeJ mice do not respond (or produce GAF?) after an intravenous injection of phenol-water lipopolysaccharide, but they react normally (produce GAF?) when given a trichloroacetic acid preparation. They also behave the same as conventional animals when injected with serum from poisoned normal mice, especially when the reticuloendothelial system of the donors has been activated by prior injections of Zymosan or heat-killed tubercle bacilli. The C3H/HeJ mice have been used, therefore, as assay animals to establish that peak levels of GAF appear in donor serum about 2 h after an injection of lipopolysaccharide, and it is produced intraperitoneally in C3H/HeJ mice given a mixture of endotoxin and peritoneal exudate cells derived from responder mice. GAF elutes from Sephadex G-200 along with markers of known molecular weight in the region of 100,000 to 200,000. It is inactivated by trypsin and by heating at 75 degrees C for 1 h.
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PMID:Elicitation of endotoxemic effects in C3H/HeJ mice with glucocorticoid antagonizing factor and partial characterization of the factor. 34 17

Heat-stable enterotoxin (ST) produced by porcine strains of enterotoxigenic (ENT+) Escherichia coli has been purified to apparent homogeneity by sequential ultrafiltration, acetone fractionation, preparative gel electrophoresis, diethylaminoethyl Bio-Gel A ion-exchange chromatography, and Bio-Gel P-10 gel filtration. The enterotoxin, purified more than 1,500-fold, exhibited a molecular weight of 4,400, as determined by both sodium dodecyl sulfate-gel electrophoresis and gel filtration. A molecular weight of 5,100, representing 47 residues, was calculated from amino acid analysis data. The amino acid content was distinctive, with an unusually high proportion of cystines and few hydrophobic amino acids. A single amino-terminal residue, glycine, was observed. Purified ST was stable to heating (100 degrees C, 30 min) and did not lose biological activity after treatment with Pronase, trypsin, proteinase K, deoxyribonuclease, ribonuclease, and phospholipase C. Periodic acid oxidation and several organic solvents (acetone, phenol, chloroform, and methanol) had no effect on the biological activity of ST. Further, purified ST was stable to acid treatment at pH 1.0 but lost biological activity at pH values greater than 9.0. Neither lipopolysaccharide nor lipid contamination was evident in purified preparations. A characteristic absorption spectrum was observed during the course of the purification, which shifted from a maximum at 260 nm in crude preparations to 270 nm for the purified toxin. Antiserum obtained from rabbits immunized with ST or ST coupled to bovine serum albumin neutralized the action of the enterotoxin in suckling mice; however, passive hemagglutination and hemolysis titer assays suggested that ST is a poor antigen.
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PMID:Purification and chemical characterization of the heat-stable enterotoxin produced by porcine strains of enterotoxigenic Escherichia coli. 34 81


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