Takenobu Y, Takaoka M, Suyama E, Yano M, Morimoto S
Department of Pharmacology, Osaka University of Pharmaceutical Sciences, Japan.
Biochem Int. 1990;21(3):417-23.
A peptide derived from rat urinary prokallikrein by trypsin treatment comprised 7 amino acids, the sequence (Ala-Pro-Pro-Val-Gln-Ser-Arg) of which was identical with that of the N-terminal region in prokallikrein. Thus, with trypsin treatment, rat urinary prokallikrein is converted to the active form with the release of the N-terminal propeptide consisting of 7 amino acids. An Arg-1-Val+1 bond in the prokallikrein was found to be the site of proteolytic cleavage of the propeptide.
经胰蛋白酶处理从大鼠尿中激肽释放酶原衍生出的一种肽由7个氨基酸组成,其序列(丙氨酸-脯氨酸-脯氨酸-缬氨酸-谷氨酰胺-丝氨酸-精氨酸)与激肽释放酶原N端区域的序列相同。因此,经胰蛋白酶处理后,大鼠尿激肽释放酶原转变为活性形式,同时释放出由7个氨基酸组成的N端前肽。已发现激肽释放酶原中的精氨酸-1-缬氨酸+1键是前肽蛋白水解切割的位点。