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:3.4.21.1 (chymotrypsin)
10,938 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Characterization of the trypsin-, chymotrypsin- and elastase-inhibiting properties of porcine serum was carried out by gel filtration on Ultrogel, AcA 44, and agarose gel electrophoresis with subsequent processing for protease-inhibiting activity. Moreover, by allowing the fractions obtained from gel filtration to react with antibodies to porcine serum protease inhibitors, the specific inhibiting properties of these inhibitor molecules were identified. At least six protease inhibitors were identified and partially characterized in porcine serum. Two alpha 2 -macroglobulins (alpha 2 Mf and alpha 2 Ms), homologues to human alpha 2 -macroglobulin, with slightly different electrophoretic mobilities, were both found to exhibit trypsin, chymotrypsin and elastase inhibiting activity. Alpha 1 -Protease inhibitor (Mr 51 000), a homologue to human alpha 1 -protease inhibitor (alpha 1 -antitrypsin), also showed trypsin-, chymotrypsin- and elastase-inhibiting properties. Inter-alpha-trypsin inhibitor (Mr 162 000 and 129000), a porcine serum counterpart to human inter-alpha-trypsin inhibitor, showed trypsin- and chymo-trypsin-inhibiting properties. In addition, a specific trypsin inhibitor, alpha 2 -antigrypsin (Mr 58 000), and a specific elastase inhibitor, beta-elastase inhibitor, were characterized in porcine serum, and these seem to have no counterparts in human serum.
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PMID:Identification and characterization of trypsin, chymotrypsin and elastase inhibitors in porcine serum. 9 64

In this paper we describe new and so far unknown protease inhibitors present in the tentacles of the annelid Sabellastarte indica Savingny. At least five different isoinhibitors with inhibitory activity towards trypsin, plasmin, chymotrypsin and kallikrein can be separated electrophoretically. Our protease inhibitor active material differs from the other well known protease inhibitors found in invertebrates in its high molecular weight, in that it is heat-labile and in the occurrence of the isoelectric point in the weakly acid region. On the other hand, the new protease inhibitors have some similarities to the soybean inhibitor described by Kunitz, and to ovomucoid. We also discuss the possibility that these inhibitors may influence the fibrinolytic system.
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PMID:[New protease-inhibitors with broad specificity in the polychaet Sabellastarte indica (Savingny), I (author's transl)]. 12 15

Resting mammalian fibroblasts, either sparse and maintained in a serum-free medium, or confluent and contact inhibited, are stimulated to divide by treatment with a preparation of 3':5'-cyclic AMP phosphodiesterase. This enzyme preparation contained a low level of trypsin-like and alpha-chymotrypsin-like activity, but its effect on cell growth could not be mimicked by pure, crystallized trypsin and alpha-chymotrypsin at concentration equivalent to their contamination in the above preparation. Preincubation of the 3':5'-cyclic AMP phosphodiesterase preparation with the protease inhibitor, phenyl methane sulfonyl fulride, did not affect, either, its stimulation of DNA synthesis in fibroblasts, or its enzymatic hydrolysis of cyclic AMP.
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PMID:Growth stimulation of sparse, serum deprived and of confluent, contact inhibited mammalian fibroblasts by a preparation of 3':5'-cyclic AMP phosphodiesterase. 19 71

Proteolytic removal of the pre-segment from growing nascent chains of pre-human placental lactogen (hPL) occurred during in vitro translation of placental mRNA if crude membranes derived from ascites lysates, dog pancreas, or rat liver rough endoplasmic reticulum were added to the translation mixtures. The cotranslational proteolytic event was inhibited by the peptide protease inhibitor, chymostatin, but not by leupeptin, antipain, or elastatinal. The proteases involved in cleavage were solubilized with detergent and converted completed pre-hPL to hPL (post-translational processing). Direct assay of the solubilized membranes, with synthetic fluorogenic aminocoumarin peptide substrates, revealed no significant tryptic or elastase-like activity, but activity against a chymotrypsin substrate [(succinyl-Ala-Ala-Phe)-7-amino-4-methyl-coumarin] was found. This activity was dependent upon both an endopeptidase and an aminopeptidase. Although bestatin inhibited the aminopeptidase activity, it had no effect on the endopeptidase or on post-translational cleavage. Although this endopeptidase cleaved on the COOH side of an alanine residue, it was not inhibited by elastatinal. However, it was inhibited by high levels of chymostatin and by some serine protease inhibitors.
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PMID:Characterization of an endopeptidase involved in pre-protein processing. 29 60

The inhibition of chymotrypsin activity by pig, dog, human and rat blood plasma was studied. N-Benzoyl-L-tyrosyl-p-amino-benzoate (PABA-peptide) was used as the substrate. Crystalline bovine chymotrypsin as well as activated lyophilized human, pig, rat and chicken pancreatic secretions were used as enzyme sources. Certain species differences were noted. Swine plasma had no effect on bovine or human chymotrypsin while it inhibited that of the chicken by 67%. Dog plasma was a potent inhibitor of chymotrypsin activity from all sources tested. An acute pancreatitis model using the rat was also developed in which pancreatic juice flow was blocked without interference with biliary flow. After 24 h, these animals had increased plasma amylase activity, decreased plasma protease inhibitor and decreased hematocrit. By 72 h, amylase, trypsin inhibitor and hematocrit had nearly recovered while chymotrypsin inhibitor had actually increased above control levels. In rats subjected to hepatectomy or to hepatectomy plus pancreatic blockage, plasma protease inhibitor was even more severely depressed and remained so.
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PMID:Species specificity and other aspects of chymotrypsin inhibition by plasma. 61 41

When pancreatic DNase I is used as a specific biochemical reagent in the preparation of nuclear ribonucleic acids or nuclear proteins, freedom from contaminating ribonucleases or proteases is an important property of the enzyme preparation. A simple one-step procedure has been developed to effect complete removal of trypsin, chymotrypsin, and chymotrypsinogen by a combination of affinity chromatography and salting-out adsorption on lima bean protease inhibitor coupled to Sepharose (a column (0.9 X 60 cm) operated in series with a regeneratable 1-ml bed). Commercial preparations of DNase (about 10 mg) give a quantitative yield of the enzyme that is protease-free as evidenced by full stability for more than 10 days at pH 8 and 37 degrees C even in the absence of the protecting action of Ca2+. Removal of the last traces of RNase has been accomplished by affinity chromatography on a column (0.4 X 72 cm) of 5'-(4-aminophenyl-phosphoryl)-uridine 2'(3')-phosphate-Sepharose; the product is a highly active DNase that gives no detectable hydrolysis of RNA by assay on radioactive substrates.
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PMID:Preparation of protease-free and ribonuclease-free pancreatic deoxyribonuclease. 70 Dec 44

An acid stable protease inhibitor was isolated from human bronchial secretion. Two important stages of the purification procedure were affinity chromatography on trypsin bound to Affi-Gel 10 and ion-exchange chromatography on SP-Sephadex C-50. The isolated inhibitor appeared as a single band on analytical disc electrophoresis and eluted as a homogeneous protein peak on gel filtration on Sephadex G-75 corresponding to a molecular weight of about 10500. Amino acid analyses showed no tryptophan or histidine and as N-terminal amino acid tyrosine. No glucosamine or galactosamine was detected. The results of the analyses suggest that the purified inhibitor is identical to the low molecular weight trypsin-chymotrypsin inhibitor of human seminal plasma (HUSI-I).
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PMID:Isolation and partial characterization of a low molecular weight acid stable protease inhibitor from human bronchial secretion. 88 Nov 64

A search for the source of the residual esterase activity of crude lima bean protease inhibitor-binding anhydrochymotrypsin preparations was undertaken. The preparations were found to contain about 40% of protein that possesses 1% (kc/Km) to 12% (kc) of the esterase activity of alpha-chymotrypsin. The active protein was isolated by affinity chromatography on soybean trypsin inhibitor-Sepharose. It appears to be an anhydroenzyme or a mixture of a limited number of anhydroenzymes in which a serine other than the catalytically essential serine-195 of the native enzyme has been converted to dehydroalanine.
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PMID:Residual esterase activity of lima bean inhibitor-binding anhydrochymotrypsin preparations. 92 2

Incorporation of amino acids into proteins in HeLa cells, virus-transformed 3T3 mouse fibroblasts, and mouse plasmacytoma cells is inhibited after the addition of L-1-tosylamido-2-phenylethyl chloromethyl ketone, an alkylating agent and chymotrypsin-specific protease inhibitor. Addition of this drug to tissue culture cells at concentrations of 20 to 30 mug per ml results in an irreversible inhibition of the incorporation of amino acids into cellular proteins, and a rapid and complete breakdown of polyribosomes. A comparative study examining the effects of L-1-tosylamido-2-phenylethyl chloromethyl ketone and several known inhibitors of in vivo protein synthesis, with known mechanisms of action, revealed that an optimal concentration of L-1-tosylamido-2-phenylethyl chloromethyl ketone: (a) immediately and selectively inhibits initiation of protein synthesis, (b) does not significantly affect normal elongation rates, and (c) does not promote a premature release of nascent peptides. L-1-Tosylamido-2-phenylethyl chloromenthyl ketone may prove to be a useful tool in investigating the initiatior of protein synthesis in eukaryotic cells.
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PMID:Inhibition of initiation of protein synthesis in mammalian tissue culture cells by L-1-tosylamido-2-phenylethyl chloromethyl ketone. 117 Jan 68

Normal human nasal fluid contains several enzymes of the intermediary metabolism as well as a specific protease inhibitor, which inhibits trypsinm chymotrypsin and leucocytic proteases. During the course of acute and chronic nasal and paransal sinus infections the inhibitor level varies. The inhibitor level is an indicator of poor healing. It is possible too, to differentiate viral rhinitis from bacterial or allergic or atrophic rhinitis by a signigicant increase of the activities of the enzymes GOT, LDH and CPK.
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PMID:The enzymology of nasal secretion. 127 12


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