人组织激肽释放酶结合蛋白的纯化及特性的研究  

Purification and Identification of a New Protein, Human Tissue Kallikrein-binding Protein, from Human Plasma

作　　者：王茂音[1] 王丽秀[2] 

机构地区：[1]安徽医科大学生化教研室 [2]上海生物化学研究所

出　　处：《安徽医科大学学报》1989年第4期253-258,共6页Acta Universitatis Medicinalis Anhui

摘　　要：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。We have recently purified and identifid a new protein, human tissue kallikrein-binding protien (KBP), from human plasma. In 2 dimentional gel elctrophoresis, KBP migrates as one protein band with isoelectric point of 5.4 Also, KBP was eluted as a single peak on reversedphase HPLC. In Western blot analysis using the antibodies generated against purified KBP, a 54 KDa protein Was identified in the purified plasma protein. In ligand blotting, this 54 KDa protein was visualized by autoradiography by its binding to ^(125)I-HUK.The purified KBP is an acidic protelnand consists of a single peptide chain with 487 amino acid residues, and with an apparent molecular weight of 54000 as determined by SDS-PAGE and by gel filtration. The purified KBP and human tissue kallikrein forms a 92 KDa SDS- and heat-stable complex. The complex formation is inhibited by the antibody in a dose dependent manner. It was presumed that KBP may playa role in the regulation of metabolism of tissue kallikrein on the level of biosynthesis and excretion.

关 键 词：血管舒缓素 蛋白 人血浆 

分 类 号：Q592[生物学—生物化学]