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)

An epidemiologic study of Pasteurella haemolytica serovar 1 (Ph1) in market-stressed feeder calves from 7 farms in eastern Tennessee was conducted. The nasal mucus of each calf was cultured sequentially at the farm of origin (day 0), at an auction market (day 133), and at a feedyard in Texas (days 141, 148, 155, and 169). Of the 103 calves tested, 77 were culture-positive, including 1 on day 0, 1 on day 133, 20 on day 141, 57 on day 148, 50 on day 155, and 14 on day 169. From the 143 Ph1 isolates, 20 enzyme profiles were determined by use of a commercial enzyme system that detects 19 enzymatic reactions; 4 antimicrobial susceptibility profiles were obtained, using the disk-diffusion method, which evaluated susceptibility to 11 antibacterial drugs. All isolates were positive for acid phosphatase and alkaline phosphatase, but were negative for alpha-galactosidase, alpha-mannosidase, beta-glucosidase, beta-glucuronidase, cystine aminopeptidase, N-acetyl-beta-glucosaminidase, and trypsin. Other positive enzyme reactions included: leucine aminopeptidase, 140 Ph1 isolates; phosphohydrolase, 90 isolates; alpha-fucosidase, 63 isolates; esterase (C4), 59 isolates; valine aminopeptidase, 30 isolates; esterase lipase (C8), 24 isolates; beta-galactosidase, 2 isolates; and alpha-glucosidase, chymotrypsin and lipase (C14), 1 isolate each. Thirty-four Ph1 profiles were identified, using combined enzyme and antimicrobial susceptibility profiles. The data indicate that the strains isolated during the feedyard period may have been determined more by farm of origin (P < or = 0.001) than by habitation with calves from other farms while in the feedyard.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Identification of Pasteurella haemolytica A1 isolates from market-stressed feeder calves by use of enzyme and antimicrobial susceptibility profiles. 842 78

In the preceding study (Okamura et al., 1992; Biol Reprod 47:1040-1052) we suggested that a 135-kDa protein secreted by porcine epididymis is involved in the sperm maturation. In this work, we have isolated the cDNA clone coding the 135-kDa protein in an effort to investigate its structure and function. The 135-kDa protein was purified from porcine cauda epididymal fluid. Three oligonucleotide probes were synthesized according to the amino acid sequences of N-termini of the native protein and trypsin-digested peptides. A cDNA clone hybridizing with these three probes was isolated from the cDNA library derived from the porcine proximal corpus epididymis. It encodes a novel protein with 1,006 amino acid residues in an open reading frame. Its overall amino acid sequence was significantly homologous (25.7%) to the alpha-mannosidase precursor of Dictiostelium discoideum (P34098). The 135-kDa protein could digest both p-nitro-phenyl-alpha-D-mannoside and high mannose oligo saccharide (Man8-GlcNAc2), strongly suggesting that it is an alpha-mannosidase homologue. The expression of this protein was specific to porcine and was localized to the very narrow parts of epididymis: the border of the caput and corpus epididymis. This protein may serve as a good marker for the functional differentiation in porcine epididymis. A possible role of this protein in the species-specific sperm-egg interaction is discussed.
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PMID:Cloning of complementary DNA encoding a 135-kilodalton protein secreted from porcine corpus epididymis and its identification as an epididymis-specific alpha-mannosidase. 856 59

The enzymatic activity of 70 feline and canine Microsporum canis isolates was determined by the Api-Zym test. The liquid phase of cultures, inoculated into Tryptic Soy Broth, was used to examine 19 enzymes. Considerable differences were observed among the extracellular enzymatic patterns. All the isolates produced alkaline phosphatase and beta-glucosidase, while lipase (C14), trypsin, chymotrypsin, beta-glucuronidase, and alpha-fucosidase activity was never revealed. Esterase (C4) activity was present in 57 samples (81%), esterase lipase (C8) in 31 (44%), leucine arylamidase in 35 (50%), valine arylamidase and cystine arylamidase in 7 (10%), acid phosphatase in 64 (91%), naphthol-AS-BI-phosphohydrolase in 60 (86%), alpha-galactosidase in 5 (7%), beta-galactosidase in 6 (8%), alpha-glucosidase in 25 (36%), N-acetyl-beta-glucosaminidase in 41 (58%), and alpha-mannosidase in 51 (73%). The beta-galactosidase activity of M. canis has not been reported previously. Remarkable variations of intensity for each enzymatic activity were also detected. It is believed that these results could provide basic data for further investigations on the pathogenic role of enzymes secreted by M. canis.
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PMID:Extracellular enzymatic activity of Microsporum canis isolates. 868 26

In this study, using the API-ZYM system, we have reported the enzyme profile of 42 soil strains and 2 clinical strains of Nocardia asteroides isolated locally. Of the 19 enzymes tested, only 7 were demonstrable in over 90% of the soil isolates. These included alkaline phosphatase, esterase lipase, leucine arylamidase, acid phosphatase, phosphohydrolase, alpha-glucosidase and beta-glucosidase. In addition, beta-galactosidase activity was demonstrated in all the strains by the O-nitrophenyl-beta-D-galactopyranoside (ONPG) test. The enzymes which were not demonstrable in > 95% of the strains included valine arylamidase, cystine arylamidase, trypsin, chymotrypsin, alpha-galactosidase, beta-glucoronidase, N-acetyl-beta-glucosaminidase, alpha-mannosidase and alpha-fucosidase. With the exception of valine arylamidase, which was lacking in all but one isolate, the enzyme profiles of the soil isolates were comparable with the clinical isolates of N. asteroides reported in previous studies. The reasons for this difference in the two sets of isolates is not clear. The study reinforces the view that specific differences in the enzymatic profiles of Nocardia species could be used for their rapid identification. However, more extensive studies are needed to establish the reproducibility of this method. To the best of our knowledge, this is the first study of the enzymatic profile of soil isolates of N. asteroides originating from a single geographic region.
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PMID:A study of the enzymatic profile of soil isolates of Nocardia asteroides. 1035 11

An N-linked glycosylation in a novel C-lectin protein from snake venom was observed by Edman degradation and liquid chromatography-electrospray mass spectrometry. The peptides obtained by trypsin cleavage were analyzed to confirm the amino acid sequence and Asn5 was found to be the N-glycosylation site. The result was further confirmed by N-glycosidase digestion. In addition, the protein and tryptic peptides with and without glycan chain were characterized by mass spectrometry according to the mass difference. The glycopeptide obtained from proteolytic digestion was analyzed and the glycoforms were identified as high-mannose type by tandem MS coupled with alpha-mannosidase digestion. An oxidized Met residue was detected and located in the protein by mass spectrometry.
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PMID:Characterization and analysis of a novel glycoprotein from snake venom using liquid chromatography-electrospray mass spectrometry and Edman degradation. 1056 75

Changes associated with blood and sugar meal digestion in the sandfly, Phlebotomus langeroni were characterized. Different types of sugars: sucrose, glucose, melibiose, cellobiose, lactose, starch, fig fruits, honey dew and a mixture of sucrose and sugar sources were used for the sandfly feeding. Activities of glycosidases and proteases in the sandfly guts after blood and sugar meals were determined using the endpoint method. The results showed that glycosidases (alpha-glycosidase, beta-glycosidase, alpha-galactosidase, and beta-galactosidase) are present in the sandfly midguts. No activities of the glycosidases (alpha-mannosidase and alpha-amylase) were detected in the sandfly gut. Proteases: trypsin and aminopeptidase showed activities in the sandfly midguts. It is concluded that the midgut glycosidase may play an important role in the vector-parasite interaction. Trypsin and aminopeptidase induction after a blood meal is controlled by a secretogogue mechanism which indirectly influences the outcome of the Leishmania parasite infection.
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PMID:Induction of some digestive enzymes in the midgut of the sandfly Phlebotomus langeroni after sugar and blood meals. 1256 9

Storage protein hydrolysis in the cotyledons of germinating mung beans (Phaseolus aureus Roxb.) was examined by histochemical techniques, and the autolytic capacity of isolated protein bodies was studied with biochemical methods. The localization of endopeptidase activity within the cotyledons was studied using an India ink-gelatin film technique. After 24 hours of imbibition, a low level of endopeptidase activity was found throughout the storage tissues of the cotyledons. A marked increase in activity was noted in cells farthest from the vascular bundles 48 to 60 hours after the start of imbibition. The decrease in storage protein followed the same spatial distribution starting in the cells farthest from the bundles. The cotyledons contain a population of cells in various stages of endopeptidase activity enhancement and storage protein degradation. A wave of endopeptidase activity moves progressively through the cotyledons towards the vascular bundles leaving behind areas devoid of stored reserves and low in endopeptidase activity. Observations on the morphology of protein bodies during germination indicate that the membrane surrounding them remains intact, while the reserves disappear. This result suggests that the protein bodies may be undergoing autolysis. To determine whether this may indeed be the case, protein bodies were isolated from the meal of mung bean seeds using an aqueous medium containing 80% glycerol. The protein body preparations and the cytoplasm were assayed for the presence of a number of enzymes which may be involved in the breakdown of the storage proteins. The protein bodies contained all, or nearly all, of the carboxypeptidase, alpha-mannosidase, N-acetyl-beta-glucosaminidase, and caseolytic activity. The cytoplasm contained all, or most, of the leucine aminopeptidase and the trypsin-like activity (benzoyl arginine-p-nitroanalide as substrate). Incubation of the isolated protein bodies resulted in the release of amino acids. An analysis of the products of hydrolysis indicated that very little, if any, storage protein was being hydrolyzed during the incubation. Hydrolysis of the storage proteins present in the protein bodies was greatly accelerated by the addition of extracts from the cotyledons of 4-day-old seedlings. The results suggest that new enzymic activities not present in the protein bodies isolated from dry seeds must either be activated or synthesized and possibly added to the protein bodies before storage protein breakdown can begin.
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PMID:Histochemical and biochemical observations on storage protein metabolism and protein body autolysis in cotyledons of germinating mung beans. 1665 90

A sexual pheromone, named the protoplast releasing substance (PRS), was formed by mating type minus cells. PRS activates mating type plus cells and results in the release and fusion of protoplasts within distended conjugation-papilla in paired cells and in the release and disruption of protoplasts in unpaired mating type plus cells. In an agar barrier system, the activation of mating type plus cells was markedly inhibited by treatment with pronase (5-10 micrograms per milliliter), proteinase (100 micrograms per milliliter), and alpha-mannosidase (10 micrograms per milliliter). Trypsin (10-100 micrograms per milliliter) had no effect on the activation in the agar barrier system. The results suggest that PRS is a glycoprotein with pronase-sensitive and trypsin-insensitive structure.
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PMID:Sexual Interaction in Heterothallic Strains of Closterium peracerosum-strigosum-littorale: Partial Characterization of a Male-Specific Sexual Pheromone, Protoplast-Releasing Substance. 1666 97

A protease inhibitor with a molecular weight of about 12,800 was purified to electrophoretic homogeneity from Daucus carota cells. The protease inhibitor was heat stable and inhibited trypsin but had no activity toward chymotrypsin or subtilisin. Nonembryogenic as well as embryogenic strains contained the inhibitor in similar amounts, but in the embryogenic strains the trypsin inhibitor was released from the cells and as a result accumulated in high concentrations in the culture medium, whereas no release of the trypsin inhibitor was found during cultivation of the nonembryogenic strains. Very low amounts of acid phosphatase or alpha-mannosidase activity were found in the culture filtrate of both embryogenic and nonembryogenic strains, which suggest that the release of the inhibitor from embryogenic strains was not due to cell lysis.
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PMID:Purification of a trypsin inhibitor secreted by embryogenic carrot cells. 1666 98

The majority of important allergenic extracts from arthropods present enzymatic activity. This activity has been studied particularly in Dermatophagoides house dust mites because of its implication in the stability and immunogenicity of extracts used as tools for the diagnosis and specific treatment of allergic diseases. Extracts from cultures of Blomia tropicalis [van Bronswijk (1973a, b). Acarologia 15:477-489, 490-505] and Blomia kulagini (Zakhvatkin 1936) were used to study enzymatic profiles during three growth periods of the mite population: latency phase, maximum mite concentration during exponential growth, and drop stage. The activities of 19 enzymes were analyzed using the Api Zym system. The results show a large variety of enzymes. Some enzymatic activity was found to be (almost) exclusively attributable to mites. The activity levels of proteases, glycosidases and lipases overlapped with the growth curve. Only phosphatase activity showed no significant change during mite growth when compared with the culture medium. We suggest that the glycosidases (beta-galactosidase, beta-glucuronidase, beta-N-acetylglucosaminidase, alpha-mannosidase and alpha-fucosidase) and proteases (leucine aminopeptidase and trypsin) may constitute suitable parameters for inclusion in the quality control process for the production of allergenic mite extracts, and may help define a new index for conducting environmental controls.
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PMID:Enzymatic analysis of Blomia tropicalis and Blomia kulagini (Acari: Echimyopodidae) allergenic extracts obtained from different phases of culture growth. 1686 79


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