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)

The purpose of the present investigation was to detect strains of small-sized oral spirochetes isolated from subgingival plaque for protease, peptidase, lipase, glycosidase, phosphatase, hyaluronidase and chondroitinsulfatase activities. The analyses were routinely carried out with cultures in the early stationary phase of growth after 4 days incubation. Both culture media and harvested spirochete cells were examined for the different enzyme activities. The enzymes were assayed by use of the API ZYM system, by p-nitroanilide derivatized peptides, and by hydrolyzing of mucopolysaccharides incorporated in solid bacterial medium. Relatively strong activities of trypsin-like enzymes, mainly bound to the cells, were observed in all strains. Similarly all strains showed acid phosphatases bound to the cells, too. Extracellular hyaluronidase- and chondroitinsulfatase activities were detected qualitatively in all strains after 7 days growth. The activities of the two mucopolysaccharide degrading enzymes almost disappeared after 10 subcultivations. Weak lipase (butyrate), higher lipase (caprylate), and weak phosphoamidase activities were observed in all cell pellets. No glycosidase activities were found. The observations are discussed by regarding the spirochetal enzymes as potential virulence factors for the development of marginal periodontitis.
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PMID:Enzyme activities from eight small-sized oral spirochetes. 301 Apr 39

The extracellular and cell-associated hydrolase profiles of a number of Pseudomonas fluorescens strains were examined with the Analytab API ZYM system. Esterase/lipase was the only strong extracellular enzyme activity detected (mean 3.33): weak esterase, lipase, and leucine aminopeptidase activities were found with some strains (mean activities of 1.08, 1.53, and 1.40, respectively). Very strong leucine aminopeptidase activity (4.5) was associated with the cells. Cell-associated trypsin, esterase/lipase, acid phosphatase, and phosphoamidase were also found. Neither extracellular nor cell-associated hydrolase profiles changed significantly when cells were grown in skim milk or mineral salts medium at either 5 or 20 degrees C. Similarly, added calcium did not seem required for synthesis of any of the enzymes. The extracellular enzyme profiles differed considerably from those of the cell-associated enzymes for all strains tested. An extracellular proteinase-deficient mutant of strain 32A (RM14) failed to produce significant quantities of extracellular esterase/lipase activity. Production of cell-associated enzymes was unaffected by the mutation. These results suggest that the Analytab API ZYM system may be useful in identifying psychrotrophs isolated from milk.
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PMID:Determination of the extracellular and cell-associated hydrolase profiles of Pseudomonas fluorescens sp. using the Analytab API ZYM system. 308 7

The enzymatic activities of 53 strains of Pseudomonas cepacia were determined by using the API ZYM system. Strong alkaline phosphatase, acid phosphatase, butyrate esterase, caprylate esterase, myristate lipase, leucine arylamidase, and phosphoamidase activities were consistently detected in all strains. Weak activities were observed for valine arylamidase, beta-glucosidase, and N-acetyl-beta-glucosaminidase. No activities could be demonstrated for cystine arylamidase, trypsin, chymotrypsin, alpha-galactosidase, beta-galactosidase, beta-glucuronidase, alpha-glucosidase, alpha-mannosidase, and alpha-fucosidase. Enzymatic activities of pseudomonads may provide useful information about their pathogenesis and information for identification of Pseudomonas species.
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PMID:Enzymatic characterization of Pseudomonas cepacia by API ZYM profile. 335 98

The enzyme activities of four strains of Legionella pneumophilia were investigated by using the API ZYM system (API System S.A., F-38390 Montalieu Vercieu, France) and synthetic substrates. Aminopeptidases were detected specifically against L-alanine, L-arginine, L-aspartic acid, L-cystine, L-glutaminic acid, glycine, L-histidine, L-isoleucine, L-leucine, L-lysine, L-methionine, L-phenylalanine, L-tryptophan, L-tyrosine, and L-valine. Furthermore, the bacteria possesses esterase activity splitting propionate, butyrate, caproate, caprylate, and caprate, but not laurate, myristate, palmitate, and stearate, esters. The enzymes studies were inhibited partially by aprotinin. No inhibition of phosphatase (pH range, 5.4 to 8.5) or of phosphoamidase was observed. Activities of arylsulfatase, chymotrypsin, trypsin, and glycosidases could not be detected.
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PMID:Enzymatic profile of Legionella pneumophilia. 616 35

The enzymatic profiles of several yeastlike organisms were studied using 19 substrates included in the API ZYM system. The isolates evaluated were: 186 Candida albicans, 19 C. stellatoidea, 4 C. tropicalis, 2 C. parapsilosis, 2 C. pseudotropicalis, 1 C. guilliermondii, 3 C. krusei, 11 Torulopsis (Candida) glabrata, 1 Cryptococcus neoformans, 2 Saccharomyces carlsbergensis, 1 Rhodotorula rubra, and 1 R. mucilaginosa. Esterase lipase (C8), leucine arylamidase, acid phosphatase, and phosphoamidase were detected in all of the isolates while trypsin and alpha-galactosidase were not found in any of the isolates using this system. The other enzymes were produced to a variable degree. The different enzymatic profiles might prove useful in the rapid differential diagnosis of genera and species of these yeastlike organisms. To this end, more extensive studies using more isolates of each species will be required, and enzymatic activity should be verified with other techniques and substrates.
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PMID:Contribution to the study of the enzymatic profiles of yeast organisms with medical interest. 631 Apr

An enzymatic profile of 20 strains of Pseudomonas maltophilia was undertaken with conventional plate tests, API ZYM, and 4-methylumbelliferyl-conjugated substrates. All strains produced DNase, RNase, arbutinase, esterases and lipases, mucinase, acid and alkaline phosphatases, alkaline pyrophosphate diesterase, phosphoamidase, beta-glucosidase, leucine arylamidase, and acetatase and were hemolytic for horse, sheep, and rabbit blood. The majority of strains produced chitinase, hyaluronidase, albuminase, valine arylamidase, trypsin, alpha- and beta-glucosidases, and N-acetyl-beta-glucosaminidase. API ZYM and 4-methylumbelliferyl-conjugated substrate assays are rapid, simple, specific, and sensitive and may be useful as diagnostic aids in the identification of P. maltophilia and other pseudomonads.
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PMID:Enzymatic profile of Pseudomonas maltophilia. 681 50

Enzymatic characterization of 48 Aeromonas hydrophila complex isolates from various sources was determined with the API ZYM system (Analytab Products, Plainview, N.Y.). All isolates lacked valine and cystine aminopeptidases, chymotrypsin, alpha-mannosidase, alpha-fucosidase, alpha-galactosidase, and beta-glucuronidase but possessed caprylate esterase-lipase, leucine aminopeptidase, acid phosphatase, phosphoamidase, and N-acetyl-beta-glucosidase. Variability was found in the presence of alkaline phosphatase, butyrate esterase, myristate lipase, trypsin, beta-galactosidase, alpha-glucosidase, and beta-glucosidase. No significant differences were evident among the enzymatic profiles of isolates from various sources.
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PMID:Enzymatic characterization of Aeromonas hydrophila complex by the API ZYM system. 681 46

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

Thirty strains of Propionibacterium acnes were grown in basal salt medium containing lecithin as a lipid substrate and in other media. The cultures were assayed for production of lipase (measured as fatty acid esterase) and other exoenzymes. Lipase was assayed spectrophotometrically; other enzymes were assayed using the API ZYM system (Analytab Products Inc., Plainview, NY). Substance for lipase were alpha- and beta-naphthol esters of propionic, butyric, valeric, caprylic, lauric, myristic, and oleic acids. All strains showed fatty acid esterase activity. Using the API ZYM system 19 enzymes were detected, 8 of which were found frequently and had high activity in most strains. Acid and alkaline phosphatases, phosphoamidase, ester lipase, trypsin-chymotrypsin-like proteases, beta-glucuronidase (80%), beta-galactosidase (80%), and N-acetyl-beta-glucosaminidase were found. Many enzymes of P. acnes appear to be adaptive, dependent on the culture substrate.
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PMID:Exoenzymes of Propionibacterium acnes. 717 37

The API ZYM system was used to investigate enzymatic activities of Legionella pneumophila and other Legionella-like organisms. Leucine aminopeptidase, alkaline and acid phosphatase, butyrate and caprylate esterase, and phosphoamidase activities were consistently detected in all strains tested. No evidence of myristate lipase, trypsin, chymotrypsin, or glycosidase activity was found.
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PMID:Enzymatic activities of Legionella pneumophila and Legionella-like organisms. 718 5


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