Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

A total of 80 oral strains of Bacteroides gingivalis, B. asaccharolyticus, B. melaninogenicus subsp. intermedius, B. melaninogenicus subsp. melaninogenicus, Capnocytophaga, Treponema denticola, and T. vincentii were characterized with the API ZYM system for 19 enzyme activities. Comparison of anaerobic and aerobic incubation with nine reference strains of these organisms showed no important differences. The key differential tests for black-pigmented Bacteroides strains and treponemes of oral origin were trypsin, alpha-glucosidase, and N-acetyl-beta-glucosaminidase. All Capnocytophaga strains produced distinctive aminopeptidase activities but varied in their glycosidic capabilities. The presence of a trypsin-like activity in B. gingivalis, T. denticola, and a group of Capnocytophaga strains may contribute to tissue destruction in periodontal disease.
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PMID:API ZYM system for identification of Bacteroides spp., Capnocytophaga spp., and spirochetes of oral origin. 676 81

Amylase, alpha- and beta-glucosidase, alpha- and beta-galactosidase, beta-fructosidase, trypsin, aminotripeptidase, leucine-aminopeptidase, prolinase, prolidase glycyl-L-leucine dipeptidase and glygylglycine dipeptidase are present in the 3rd instar larvae of Chilo auricilius.
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PMID:Digestive enzymes in the gut and salivary gland of the larvae of Chilo auricilius Ddgn. 698 21

The brush border of the enterocytes of the rat was isolated by the method of differential centrifugation with CaCl2 according to Schmitz. This material was solubilized with papain, trypsin and Triton X-100. The greatest amount of membrane enzymes was released to the supernatant (105 000 X g) with the use of Triton X-100. The tritonized supernatant was treated in the next step by papain, bromelain, ficin and trypsin (individually or in combinations). After simultaneous proteolysis with papain and bromelain a partial separation of the aminopeptidase from the endopeptidase by Sephadex G-200 chromatography was observed. These two enzyme activities were distinctly separated by isoelectric focusing at pH 4--6. Two enzymatically active bands (RF 0.13 and 0.24) in the aminopeptidase fraction and one single active band (RF 0.16) in the endopeptidase fraction using polyacrylamide gel electrophoresis were found. Co-migrating proteins to all of these activities were detected. Endopeptidase activity splits 3-carboxypropionyltrialanin-4-nitroanilide (SucAla3NAp) in the position P2-P1. Liberated aminoacyl-NAP may be further split to generate chromogenic 4-nitroaniline through aminopeptidase activity. Endopeptidase of the brush border of the rat enterocytes is characterized by the following properties: 1) molecular mass 130000 +/- 15 000 dalton; 2) Km value (substrate: SucAla3NAp) 1.1 X 10(-3) M; 3) pI 5.23; 4) ph optimum 8.5; 5) 50% activity remains after 15 min of preincubation at 50 degrees C; 6) activity is strongly inhibited by EDTA, p-chloromercuribenzoate, Mn2 and Co2.
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PMID:Endopeptidase of the brush border membrane of rat enterocyte. Separation from aminopeptidase and partial characterization. 700 58

The API ZYM system (Analytab Products, Plainview, N.Y.), containing 19 chromogenic substrates, was utilized semiquantitatively to detect extracellular acid and alkaline phosphatases, aminopeptidases, proteases, esterase-lipase, phosphoamidase, and glycosidases in 128 oral and nonoral isolates of black-pigmented Bacteroides, Actinobacillus, Haemophilus aphrophilus, Capnocytophaga, Fusobacterium nucleatum, Wolinella recta, and Veillonella parvula. In the black-pigmented Bacteroides group of organisms, a strong trypsin reaction was present in Bacteroides gingivalis (oral species) but not in Bacteroides asaccharolyticus (nonoral species). Bacteroides melaninogenicus subsp. melaninogenicus, in contrast to Bacteroides melaninogenicus subsp. intermedius, exhibited strong N-acetyl-beta-glucosaminidase activity. H. aphrophilus produced beta-galactosidase and alpha-glucosidase, but the closely related Actinobacillus actinomycetemcomitans did not. Capnocytophaga was distinct with respect to strong aminopeptidase reactions. This study showed that a wide range of enzymes which have the potential of causing tissue injury and inflammation can be elaborated from major oral gram-negative species. Also, the API ZYM system appears to be a valuable adjunct to traditional biochemical testing in identifying oral gram-negative species.
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PMID:Enzymatic characterization of some oral and nonoral gram-negative bacteria with the API ZYM system. 702 98

The substrate specificity of proteinase B (EC 3.4.22.9) from Baker's yeast was studied. Experiments with unblocked synthetic peptides indicated that the enzyme has no aminopeptidase activity. The proteinase cleaves trypsin substrates like Bz-Arg-OEt, Bz-Arg-pNA and Bz-Ile-Glu-Gly-Arg-pNA and chymotrypsin substrates like Ac-Tyr-OEt and Bz-Tyr-pNA. The Km value for Ac-Tyr-OEt is similar to that of chymotrypsin A, but the catalytic activity per mol proteinase B amounts to only 1/20 that of chymotrypsin A. Km and kcat for Bz-Arg-OEt are 1/50 and 1/7 as high as the corresponding values determined for trypsin. Proteinase B cleaved the oxidized insulin B chain with an initial rapid cleavage step at Leu(15)-Tyr(16) and Phe(24)-Phe(25). Slower hydrolysis was observed at Gln(4)-His(5), Leu(11)-Val(12) Tyr(16)-Leu(17), Leu(17)-Val(18), Arg(22)-Gly(23) and Phe(25)-Tyr(26). These results suggest that the specificity of proteinase B is comparable to the specificity of porcine chymotrypsin C as well as of trypsin. When the hexapeptide Leu-Trp-Met-Arg-Phe-Ala was used as a substrate for proteinase B, the enzyme preferentially attacked at Arg-Phe and more slowly at Trp-Met.
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PMID:The substrate specificity of proteinase B from baker's yeast. 702 21

The insertion of pig intestinal microvillus aminopeptidase (EC 3.4.11.2) into the membrane was studied by the hydrophobic photolabel [125I]iodonaphthylazide. The aminopeptidase was either labelled in the microvillus membrane and purified, or labelled after detergent solubilization and purification in a buffer containing Triton X-100, and then isolated from the reaction mixture. Of the three subunits A (Mr 162000), B (Mr 123000) and C (Mr 62000) of the aminopeptidase, A and B, but not C contained radioactivity, indicating that both subunit A and B carry anchoring peptide. The radioactivity when released from the subunits by trypsin treatment was connected to low-molecular-weight material.
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PMID:The insertion of pig microvillus aminopeptidase into the membrane as probed by [125I]iodonaphthylazide. 705 91

Two amphiphilic forms of intestinal microvillus aminopeptidase were obtained by purification of the enzyme in the absence and in the presence of aprotinin respectively. By subsequent treatment with trypsin in vitro a hydrophilic form was obtained. These three enzyme preparations all contained three subunits. A, B and C (molecular weight 168000, 11800 and 54000 respectively). The individual subunits were purified by gel filtration on Ultrogel AcA 22 in the presence of sodium dodecyl sulphate. Subunits A and B from aminopeptidase prepared in the presence of aprotinin contained both N-terminal lysine and alanine, whereas N-terminal alanine and glycine were found for both of these subunits from the other amphiphilic form. Conversion of amphiphilic aminopeptidase to the hydrophilic form in vitro led only to a change in the N terminus of the B subunit to a valine. N-terminal serine was found in subunit C from all three forms of the aminopeptidase. The amino acid composition and peptide maps of the isolated subunits from one of the amphiphilic forms are reported. It is suggested that subunit B and C arise by cleavage of subunit A, whereas it seemed unlikely that C originates from B. Brush border membrane vesicles were cross-linked by dimethyl-3,3-dithiobispropionimidate, and the aminopeptidase subsequently isolated. Analysis of molecular weights and subunit composition of its constituent polypeptide complexes by two-dimensional polyacrylamide slab gel electrophoresis in the presence of sodium dodecyl sulphate showed that AB, BBC, BCC, BB, BC and CC complexes had been formed. The subunit structures ABC and BBCC were thus proposed in agreement with the maximum molecular weight of the membrane-bound enzyme previously determined as 330000.U
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PMID:Structural studies on microvillus aminopeptidase from pig small intestine. 714 Jul 40

The blood-digestion kinetics of Anopheles albitarsis, An. aquasalis, An. bellator and An. homunculus were determined in the laboratory using females collected from two field sites in Trinidad. Anopheles aquasalis displayed the highest rate of haemolysis (giving an absorbance of 0.36 at 410 nm), followed by An. albitarsis (0.16), An. bellator (0.07) and An. homunculus (0.05). Trypsin activity peaked 12-24 h after blood feeding and then declined to zero at 60 h in all four species. Anopheles albitarsis had significantly higher maximum trypsin activity (0.69 units) than An. aquasalis (0.28), An. bellator (0.18) or An. homunculus (0.12) (P < 0.01). Aminopeptidase activity patterns were similar for An. aquasalis, An. bellator and An. homunculus, with peak activity at 18 h. Among the An. albitarsis mosquitoes, peak aminopeptidase activity occurred at 24 h. The peritrophic membrane developed 18, 30, 30 and 36 h post-feeding in An. aquasalis, An. albitarsis, An. bellator and An. homunculus, respectively. Stage V ovarian follicles began to mature 36 h after An. albitarsis and An. bellator fed to repletion and after 48 h in An. aquasalis and An. homunculus. Ovarian development in the four species was not affected by patterns of erythrocyte haemolysis, proteolytic enzyme activity or peritrophic-membrane development. The inter- and intra-specific variations observed in the blood-processing physiology of the four species of Anopheles are briefly discussed in terms of phylogeny.
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PMID:Blood-digestion kinetics of four Anopheles species from Trinidad, West Indies. 749 67

The principal digestive proteinases of the gypsy moth, Lymantria dispar, larval midgut were identified, and the subcellular distribution of the enzyme activities was determined. Proteinase activities of fifth-instar larvae were largely attributed to two luminal serine proteinases, a trypsin-like enzyme (TLE) and an elastase 2-like enzyme (ELA). TLE was purified to homegeneity by benzamidine-Sepharose affinity chromatography. With respect to size (M(r) = 25 kDa), substrate specificity, and interaction with trypsin inhibitors, the gypsy moth enzyme resembled mammalian pancreatic trypsin and trypsin-like enzymes from other insects. Gypsy moth elastase (ELA) was purified from the benzamidine-Sepharose flow-through by mono-Q FPLC. ELA exhibited a slightly smaller size (M(r) = 24 kDa) than TLE. The insect enzyme was inhibited by DFP and chymostatin but was unaffected by TPCK. ELA exhibited little esterolytic activity with BTEE. Succinyl-Ala-Ala-Pro-Leu p-nitroanilide was one of the best substrates for ELA, which is characteristic of elastase 2. TLE and ELA constituted c. 6% of the total soluble protein in midgut lumen of actively feeding fifth-instar larvae. Chymotrypsin and carboxypeptidase activities were not detected in any midgut fraction examined. The brush border membrane (BBM) leucine aminopeptidase (LAP) was isolated from CHAPS-solubilized BBM by FPLC. SDS-PAGE results indicated that the aminopeptidase has an apparent molecular size of c. 100 kDa. The aminopeptidase was inhibited by bestatin and was unaffected by serine proteinase inhibitors.
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PMID:Gypsy moth midgut proteinases: purification and characterization of luminal trypsin, elastase and the brush border membrane leucine aminopeptidase. 771 46

The survey is devoted to the description of properties of proteolytic enzymes of some sea organisms. Structure peculiarities and properties of proteinases of trypsin and chymotrypsin type, carboxypeptidases A and B, aminopeptidase and leucine aminopeptidase of molluscs, stars, shrimps, fishes and other sea organisms have been considered. Data are presented about trypsins typical of the sea organisms which are characterized by high content of asparaginic and glutaminic acids and small values of activation energy of the reactions which they catalyse. Data are discussed concerning stability of enzymes as to heat denaturation, effect of the environment with external values of pH. Based on the similarity of the substrate specificity of enzymes, their sensitivity to inhibitors, it is concluded that the enzymes of the sea organisms and mammals are similar.
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PMID:[Peptide hydrolases of marine organisms]. 778 82


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