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http://purl.uniprot.org/citations/2404007http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2404007http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2404007http://www.w3.org/2000/01/rdf-schema#comment"Human alpha 1-antichymotrypsin has been cloned, sequenced and expressed in Escherichia coli and recombinant protein as well as point-specific mutants have been purified and characterized. The corrected gene-deduced amino acid sequence has 45% overall identity with alpha 1-protease inhibitor, which is higher than the 42% previously reported (Chandra, T., Stackhouse, R., Kidd, V. J., Robson, J. H., and Woo, S. L. C. (1983) Biochemistry 22, 5055-5060). Recombinant antichymotrypsin (rACT) is similar to natural antichymotrypsin with respect to the specificity of its interactions with proteases. Its second-order rate constant for association with bovine chymotrypsin is 6-8 x 10(5) M-1 s-1, which is identical to that of the serum-derived inhibitor. Site-specific mutagenesis has been used to produce two variants of rACT in which the P1 position has been changed from leucine to either methionine (L358M-rACT) or arginine (L358R-rACT). L358M-rACT has a specificity of inhibitory activity toward serine proteases closely similar to that of native rACT. By contrast, the specificity of L358R-rACT is quite different from that of native rACT, most notably in efficiently inhibiting trypsin and human thrombin while showing a decreased ability to inhibit chymotrypsin."xsd:string
http://purl.uniprot.org/citations/2404007http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(19)40178-6"xsd:string
http://purl.uniprot.org/citations/2404007http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(19)40178-6"xsd:string
http://purl.uniprot.org/citations/2404007http://purl.uniprot.org/core/author"Wang Z."xsd:string
http://purl.uniprot.org/citations/2404007http://purl.uniprot.org/core/author"Wang Z."xsd:string
http://purl.uniprot.org/citations/2404007http://purl.uniprot.org/core/author"Rubin H."xsd:string
http://purl.uniprot.org/citations/2404007http://purl.uniprot.org/core/author"Rubin H."xsd:string
http://purl.uniprot.org/citations/2404007http://purl.uniprot.org/core/author"Johnson J.L."xsd:string
http://purl.uniprot.org/citations/2404007http://purl.uniprot.org/core/author"Johnson J.L."xsd:string
http://purl.uniprot.org/citations/2404007http://purl.uniprot.org/core/author"Cooperman B.S."xsd:string
http://purl.uniprot.org/citations/2404007http://purl.uniprot.org/core/author"Cooperman B.S."xsd:string
http://purl.uniprot.org/citations/2404007http://purl.uniprot.org/core/author"McLarney S."xsd:string
http://purl.uniprot.org/citations/2404007http://purl.uniprot.org/core/author"McLarney S."xsd:string
http://purl.uniprot.org/citations/2404007http://purl.uniprot.org/core/author"Naidoo N."xsd:string
http://purl.uniprot.org/citations/2404007http://purl.uniprot.org/core/author"Naidoo N."xsd:string
http://purl.uniprot.org/citations/2404007http://purl.uniprot.org/core/author"Nickbarg E.B."xsd:string
http://purl.uniprot.org/citations/2404007http://purl.uniprot.org/core/author"Nickbarg E.B."xsd:string
http://purl.uniprot.org/citations/2404007http://purl.uniprot.org/core/author"Schoenberger O.L."xsd:string
http://purl.uniprot.org/citations/2404007http://purl.uniprot.org/core/author"Schoenberger O.L."xsd:string
http://purl.uniprot.org/citations/2404007http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/2404007http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/2404007http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/2404007http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string