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在人胰液中鉴定出一种羧肽酶原A截短型蛋白酶E二元复合物。

Identification of a procarboxypeptidase A-truncated protease E binary complex in human pancreatic juice.

作者信息

Moulard M, Kerfelec B, Mallet B, Chapus C

机构信息

Centre de Biochimie et de Biologie Moléculaire du CNRS, Marseille, France.

出版信息

FEBS Lett. 1989 Jul 3;250(2):166-70. doi: 10.1016/0014-5793(89)80712-4.

Abstract

The characterization, in human pancreatic juice, of a binary complex associating procarboxypeptidase A with a 32 kDa inactive glycoprotein (G32) is reported in this paper. Free G32 was isolated after dissociation of the binary complex. N-terminal sequence analysis revealed a complete homology between this protein and human protease E (HPE 1), except for the two strongly hydrophobic N-terminal residues (Val-Val) which are missing in G32. This protein might be a truncated protease E highly analogous to the subunit III of the ruminant procarboxypeptidase A-S6 ternary complex. The analogy with bovine subunit III is further supported by interspecies reassociation experiments showing that bovine procarboxypeptidase A can specifically bind human G32.

摘要

本文报道了在人胰液中一种将羧肽酶原A与一种32 kDa无活性糖蛋白(G32)结合的二元复合物的特性。二元复合物解离后分离出游离的G32。N端序列分析显示,该蛋白与人类蛋白酶E(HPE 1)完全同源,但G32中缺少两个强疏水的N端残基(Val-Val)。该蛋白可能是一种截短的蛋白酶E,与反刍动物羧肽酶原A-S6三元复合物的亚基III高度相似。种间重结合实验表明牛羧肽酶原A能特异性结合人G32,这进一步支持了其与牛亚基III的相似性。

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