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α1-硫醇蛋白酶抑制剂的纯化与特性鉴定及其与激肽和无片段1.2的高分子量激肽原的同一性

Purification and characterization of alpha 1-thiol proteinase inhibitor and its identity with kinin- and fragment 1.2-free high molecular weight kininogen.

作者信息

Ohkubo I, Namikawa C, Higashiyama S, Sasaki M, Minowa O, Mizuno Y, Shiokawa H

机构信息

Department of Biochemistry, Nagoya City University Medical School, Japan.

出版信息

Int J Biochem. 1988;20(3):243-58. doi: 10.1016/0020-711x(88)90348-5.

Abstract
  1. alpha 1-Thiol proteinase inhibitor (alpha 1 TPI) purified from outdated human plasma was a glycoprotein with Mr 83,000 and was composed of heavy and light chains held together with a disulfide bond. 2. The data on amino acid composition, amino terminal sequence of the light chain and carboxyl terminal sequences of the heavy and light chains indicate that alpha 1 TPI is identical with kinin- and fragment 1.2-free HMW kininogen. 3. Purified human plasmin generated a derivative having the same molecular weight (Mr 83,000), same subunit structure (heavy and light chains) and same inhibitory capacity as alpha 1 TPI from HMW kininogen and kinin-free HMW kininogen. This indicated the possibility that alpha 1 TPI is derived from HMW kininogen by plasmin.
摘要
  1. 从过期人血浆中纯化得到的α1-硫醇蛋白酶抑制剂(α1TPI)是一种糖蛋白,分子量为83,000,由通过二硫键连接的重链和轻链组成。2. 关于氨基酸组成、轻链的氨基末端序列以及重链和轻链的羧基末端序列的数据表明,α1TPI与激肽和无片段1.2的高分子量激肽原相同。3. 纯化的人纤溶酶从高分子量激肽原和无激肽高分子量激肽原产生了一种衍生物,其分子量(83,000)、亚基结构(重链和轻链)和抑制能力与α1TPI相同。这表明α1TPI可能是由纤溶酶从高分子量激肽原衍生而来的。

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