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从豚鼠血浆中纯化和鉴定血浆激肽释放酶的新型底物PK-120。

Purification and characterization of PK-120, a novel substrate for plasma kallikrein, from guinea pig plasma.

作者信息

Pu X P, Nagasawa S

机构信息

Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.

出版信息

Biol Pharm Bull. 1995 Jun;18(6):837-41. doi: 10.1248/bpb.18.837.

Abstract

PK-120 is a novel substrate of plasma kallikrein isolated from human plasma. Western blotting using anti-human PK-120 polyclonal antibodies demonstrated the presence of a PK-120-like protein in guinea pig, rat and mouse plasma. We purified the immunoreactive-120 kDa protein from guinea pig plasma by polyethylene glycol fractionation followed by ion-exchange chromatography using Q-Sepharose, heparin-Sepharose, Mono-Q and gel filtration with TSK G3000. The 120 kDa protein thus isolated was similar to human PK-120 with respect to limited proteolysis by kallikrein, amino acid composition, and the N-terminal amino acid sequence, indicating that the immunoreactive 120 kDa protein was guinea pig PK-120.

摘要

PK - 120是一种从人血浆中分离出的新型血浆激肽释放酶底物。使用抗人PK - 120多克隆抗体进行的蛋白质印迹法显示,豚鼠、大鼠和小鼠血浆中存在一种PK - 120样蛋白。我们通过聚乙二醇分级分离从豚鼠血浆中纯化了免疫反应性120 kDa蛋白,随后使用Q - Sepharose、肝素 - Sepharose、Mono - Q进行离子交换色谱,并使用TSK G3000进行凝胶过滤。如此分离出的120 kDa蛋白在激肽释放酶有限的蛋白水解、氨基酸组成和N端氨基酸序列方面与人PK - 120相似,表明免疫反应性120 kDa蛋白是豚鼠PK - 120。

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