Cloning of the gene and cDNA for human heart chymase.

摘要: We have recently identified and characterized a chymotrypsin-like serine proteinase in human heart (human chymase) that is the most catalytically efficient enzyme described, thus far, for cleavage of angiotensin I to yield II dipeptide His-Leu. Compared other chymases, this also has an unusually high degree specificity substrate I. report here molecular cloning nucleotide sequence gene cDNA encoding chymase, determination its entire deduced amino acid sequence. These data indicate chymase highly homologous members subfamily proteinases and, likely, all evolved from common ancestral gene. Potential regulatory elements found 5'-untranslated region chymases are However, lacks mast cell-specific sequences 5'- 3'-untranslated regions rat In addition, contains clusters unique located at key positions likely involved binding, which may contribute specificity. contrasting features cDNA, potential determinants primary structure underlie functional characteristics considered.