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作者首次从人血浆中提纯了一种新发现的蛋白质——组织激肽释放酶结合蛋白(KBP),并对其某些生化特性作了初步的研究。提纯物的逆相HPLC图谱为一单一蛋白峰,并经魏氏试验鉴定,证明所提纯的蛋白质为组织激肽释放酶结合蛋白。KBP是一种酸性蛋白质,由487氨基酸残基所组成,分子量约54KDa,pI=5.4。纯化的KBP特异地和~(125)I-HUK结合成92KDa的复合物,复合物的形成具有明显的特异性,KBP不能和前激肽释放酶结合。推测KBP可能在合成和分泌的水平上,对组织激肽释放酶的代谢及活性起调节作用。
The authors first purified a newly discovered protein, kallikrein binding protein (KBP), from human plasma and conducted a preliminary study of some of its biochemical properties. The reverse phase HPLC chromatogram of the purified product was a single protein peak, which was identified by Weisberg test. It was proved that the purified protein was tissue kallikrein binding protein. KBP is an acidic protein consisting of 487 amino acid residues with a molecular weight of about 54 kDa and pI = 5.4. The purified KBP specifically binds to ~ (125) I-HUK to form a 92 kDa complex with distinct specificity and KBP can not bind to prekallikrein. It is speculated that KBP may play a regulatory role in the metabolism and activity of tissue kallikrein at the level of synthesis and secretion.