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T-激肽的分离与结构

Isolation and structure of T-kinin.

作者信息

Okamoto H, Greenbaum L M

出版信息

Biochem Biophys Res Commun. 1983 Apr 29;112(2):701-8. doi: 10.1016/0006-291x(83)91519-x.

Abstract

T-kinin, a previously undescribed peptide containing bradykinin, has been isolated following treatment of rat plasma with trypsin (1 mg/ml). The liberated T-kinin, which contracts the rat uterus, was isolated by procedures including OM-cellulose, Biogel P-4 and reverse-phase high-performance liquid chromatography. The final material had a single N-terminal isoleucine and was shown by amino acid analysis and sequence determination to have the structure of the undecapeptide Ile-Ser-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg (isoleucyl-seryl-bradykinin). The relationships of the protein from which T-kinin is cleaved (T-kininogen) to other known kininogens is discussed.

摘要

T-激肽是一种先前未被描述的含缓激肽的肽,在用胰蛋白酶(1毫克/毫升)处理大鼠血浆后被分离出来。释放出的能使大鼠子宫收缩的T-激肽,通过包括OM-纤维素、生物凝胶P-4和反相高效液相色谱在内的方法进行分离。最终产物的N端为单一异亮氨酸,经氨基酸分析和序列测定表明其具有十一肽Ile-Ser-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg(异亮氨酰-丝氨酰-缓激肽)的结构。文中还讨论了T-激肽从中裂解出来的蛋白质(T-激肽原)与其他已知激肽原的关系。

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