Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.1 (chymotrypsin)
 10,938 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Activities of hydrolytic enzymes on the surface of monkey kidney, canine kidney, L. FM3A and various tumor cells were determined and compared with those in the cell homogenate. Although aminopeptidase (EC 3.4.11.-) activities were always detected on the surface membrane in mammalian cells, trypsin, chymotrypsin and elastase activities were not detected while slight glycosidase activity was detected in a suspension of cultured cells. The activities of alanine-, leucine-, methionine- and phenylalanine-aminopeptidases were rather high but aminopeptidase A, proline-, valine-, glycyl propline dipeptidyl-and glycyl propyl leucine-tripeptidyl-aminopeptidases showed relatively low activities. Aminopeptidase activity was also demonstrated in the isolated membrane fractions. The specific activities of enzymes in these membrane fractions were not significantly greater than in cell homogenate so it was concluded that these enzyme activities were rather loosely bound to the cell membrane. Further evidence for the localization of the aminopeptidase activities on the cell surface was obtained by using glass-bead-bound substrate and detecting the release of the terminal residues. When bestatin, a specific inhibitor against aminopeptidase B and leucine aminopeptidase, was included in the assay system for the enzyme activities on the cell surface, the enzymes were commonly inhibited in all types of cells.
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PMID:Aminopeptidase activities on the surface of mammalian cells. 99 Mar 9

Aminopeptidase (AP) A, B, and M, gamma-glutamyltranspeptidase (GGT), endopeptidase I and II, membrane-associated endopeptidase I and II, dipeptidylaminopeptidase (DAP) I, II, and IV, trypsin and chymotrypsin were investigated with 4-methoxy-2-naphthylamine (MNA) substrates and ester proteinases with n-acetyl-L-methionine-1-naphthylester as substrate in the digestive tract of laboratory rodents. Biochemically, proteinases and ester proteinases show different activities in the salivary glands, esophagus, stomach, liver, pancreas, duodenum jejunum, ileum, and colon; sex differences in proteinase and ester proteinase activity were measured, especially in the submandibular gland of rats and mice. Histochemically these enzymes are preferentially localized in surface membranes, lysosomes, secretion granules, and Golgi apparatus of cells of the endocrine and exocrine secretory system, resorptive system and immune system of the digestive tract. Besides the general occurrence of lysosomal (DAP I and II, single cell types and functional units of these systems possess their own individual proteinase and ester proteinase equipment. The cells of the granulated tubules of rat and mouse submandibular gland contain endopeptidase I and ester proteinases, its acinar cells DAP IV, the chief cells of the stomach APA, enteroendocrine cells APA, APM, and DAP II, hepatocytes DAP IV or GGT and DAP IV, lymphocytes GGT and DAP IV, and enterocytes trypsin, chymotrypsin, and membrane-associated endopeptidase I and II. Sex differences in proteinase activity are most conspicuous in the granulated tubule cells of the rat and mouse submandibular gland. The data suggest that proteinases and ester proteinases are involved in specific functions of the cells of the digestive tract. Furthermore, myoepithelial cells, smooth muscle cells of the muscular layer of the stomach and intestine, connective tissue cells (including mast cells) and fibers, nerve cells of the myenteric plexus and the capillary bed of the digestive organs are equipped with some of these proteinases and with ester proteinases and show organ differences.
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PMID:Investigation of proteinases in the digestive tract using 4-methoxy-2-naphthylamine (MNA) substrates. 701 83

Bloodmeal digestion in midguts of the sandflies Phlebotomus papatasi and Phlebotomus langeroni (Diptera: Psychodidae) was investigated in optimized assays to detect general protease, trypsin and aminopeptidase activities using synthetic substrates. Optimal activity occurred at pH 8-9 for all enzymes examined in both species. Protease activity peaked at 24-34 h post human bloodmeal in midguts of P. papatasi and 34-48 h in P. langeroni; all endo- and exoprotease activities were completed by 50 h in P. papatasi compared to 72 h in P. langeroni. Hydrolysis of two chymotrypsin substrates was < 2% of trypsin activity in both species. Aminopeptidase activity was associated mainly with the midgut wall, whereas trypsin activity was confined to the midgut lumen. A feature of digestion in P. langeroni was the high level of aminopeptidase recorded within 10 h of the bloodmeal.
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PMID:Bloodmeal digestion in the midgut of Phlebotomus papatasi and Phlebotomus langeroni. 836 57

Wild relatives of crops are an important source of resistance genes against insect pests. However, it is important to identify the accessions of wild relatives with different mechanisms of resistance to broaden the basis and increase the levels of resistance to insect pests. Therefore, we evaluated 15 accessions of wild relatives of chickpea belonging to seven species and five genotypes of cultivated chickpea for their resistance to pod borer, Helicoverpa armigera, which is the most damaging pest of chickpea. The test genotypes were evaluated for resistance to H. armigera using detached pod assay. Data were also recorded on activity of the digestive enzymes in the midgut of the larvae fed on different wild relatives of chickpea. All the wild chickpea genotypes suffered lower pod damage and weight gained by the third-instar larvae of H. armigera was lower when fed on them compared with the cultivated chickpea. The accessions, IG 69979 (Cicer cuneatum), PI 599066, IG 70006, IG 70018, IG 70022 (Cicer bijugum), IG 599076 (Cicer chrossanicum), and IG 72933, IG 72953 (Cicer reticulatum), showed high levels of resistance to H. armigera. There were significant differences in protease activity in larval gut of H. armigera fed on different wild relatives of chickpea. Total protease, trypsin, and chymotrypsin activities were lowest in larva fed on PI 599066 (C. bijugum) compared with that in the larvae fed IG 69979 (C. cuneatum) and IG 70022 (C. bijugum). Aminopeptidase activity was highest in the larvae fed on IG 70022 (C. bijugum) and IG 599076 (C. chrossanicum), whereas lowest activity was recorded in the larvae fed on ICC 3137 and KAK 2 (susceptible checks). The variation in protease activities may be due to the presence of protease inhibitors in the wild relatives or hyperproduction of enzymes by the larvae as result of protease inhibitor activity of the wild relatives, resulting in low weight gain by larvae. The results suggested that wild relatives of chickpea with diverse mechanisms of resistance can be exploited to increase the levels and diversify the basis of resistance to H. armigera in cultivated chickpea.
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PMID:Proteolytic Activity in the Midgut of Helicoverpa armigera (Noctuidae: Lepidoptera) Larvae Fed on Wild Relatives of Chickpea, Cicer arietinum. 2992 50

The southern green stink bug, Nezara viridula is a polyphagous pest of commercially important crops during both nymph and adult stages. This insect has recently transitioned from a secondary agricultural pest to one of primary concern. Novel management solutions are needed due to the limited effectiveness of current control strategies. We performed biochemical and transcriptomic analyses to characterize digestive enzymes in the salivary glands and along midgut tissues of N. viridula nymphs and adults fed on sweet corn. The digestive profiles were more distinct between midgut regions (M1 to M3) than between life stages. Aminopeptidase and chymotrypsin activities declined from the M1 (anterior) toward the M3 midgut region. Cysteine protease activity was higher in the M2 and M3 regions than in M1. Differences in sensitivity to chymotrypsin inhibitors between midgut regions suggest that distinct genes or isoforms are expressed in different regions of the gut. In nymphs, DNA and RNA degradation was higher in M1 than in M3. Adult nuclease activity was low across all midgut regions, but high in salivary glands. The differences in protease activities are reflected by transcriptomic data and functional enrichment of GO terms. Together, our results show that different regions of the digestive tract of N. viridula have specific and distinct digestive properties, and increase our understanding of the physiology of this organism.
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PMID:Proteases and nucleases across midgut tissues of Nezara viridula (Hemiptera:Pentatomidae) display distinct activity profiles that are conserved through life stages. 3161 Jan 85