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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
1989-3-24
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pubmed:abstractText |
Previous studies with trans-4-(guanidinomethyl)cyclohexanecarboxylic acid 4-tert-butylphenyl ester (GMCHA-OPhBut), a trypsin inhibitor, strongly suggested the involvement of a trypsin-like protease in histamine release from mast cells induced by various secretagogues (Takei, M., Matumoto, T., Endo, K. & Muramatu, M. (1988) Agents and Actions, in press; Takei, M., Matumoto, T., Ito, T., Endo, K. & Muramatu, M.; Takei, M., Matumoto, T., Endo, K. & Muramatu, M. and Takei, M., Matumoto, T., Urashima, H., Endo, K. & Muramatu, M., unpublished results). Two serine proteases, chymase (Benditt, E.F. & Arase, M. (1959) J. Exp. Med. 110, 451-460) and tryptase Kido, H., Fukusen, N. & Katunuma, N. (1985) Arch. Biochem. Biophys. 239, 436-443) were demonstrated in rat peritoneal mast cells. Both enzymes were purified and the effects of inhibitors for trypsin and chymotrypsin on these proteases were examined. The trypsin-like protease was found in saline extract and purified by successive chromatographies on Sephadex G-100 and DEAE-cellulose columns. The molecular mass of this protease was apparently 120,000 Da. This protease showed maximal activity at pH 7.1 and was named pH 7 tryptase. Chymase was obtained from 1.5M NaCl extract. pH 7 Tryptase markedly hydrolysed Boc-Phe-Ser-Arg-NH-Mec and Boc-Val-Pro-Arg-NH-Mec among the various substrates containing arginyl and lysyl bonds but did not cleave Tos-Arg-OMe. Tos-Lys-CH2Cl and diisopropylfluorophosphate strongly inhibited this protease. Various inhibitors for trypsin inhibited pH 7 tryptase, and those for chymotrypsin inhibited chymase. Among the esters of GMCHA examined, GMCHA-OPhBut most strongly and competitively inhibited pH 7 tryptase but it had no effect on chymase.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chymases,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Proteinase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/tosylarginine methyl ester hydrolase
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0177-3593
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
369
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
617-25
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3066368-Animals,
pubmed-meshheading:3066368-Chromatography, DEAE-Cellulose,
pubmed-meshheading:3066368-Chromatography, Gel,
pubmed-meshheading:3066368-Chymases,
pubmed-meshheading:3066368-Hydrogen-Ion Concentration,
pubmed-meshheading:3066368-Kinetics,
pubmed-meshheading:3066368-Male,
pubmed-meshheading:3066368-Mast Cells,
pubmed-meshheading:3066368-Peptide Hydrolases,
pubmed-meshheading:3066368-Protease Inhibitors,
pubmed-meshheading:3066368-Rats,
pubmed-meshheading:3066368-Rats, Inbred Strains,
pubmed-meshheading:3066368-Serine Endopeptidases,
pubmed-meshheading:3066368-Serine Proteinase Inhibitors,
pubmed-meshheading:3066368-Structure-Activity Relationship,
pubmed-meshheading:3066368-Substrate Specificity
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pubmed:year |
1988
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pubmed:articleTitle |
Tryptase in rat mast cells: properties and inhibition by various inhibitors in comparison with chymase.
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pubmed:affiliation |
Faculty of Pharmacy, Tokushima Bunri University.
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pubmed:publicationType |
Journal Article,
Comparative Study
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