一种淋巴瘤蛋白，其体外酪氨酸磷酸化位点与pp60src中的位点同源。

A lymphoma protein with an in vitro site of tyrosine phosphorylation homologous to that in pp60src.

作者信息

Casnellie J E, Harrison M L, Hellstrom K E, Krebs E G

出版信息

J Biol Chem. 1982 Dec 10;257(23):13877-9.

Abstract

The major in vitro substrate for a tyrosine protein kinase in the particulate fraction of the lymphoma cell line LSTRA is a protein of molecular weight of 58,000 (pp58) (Casnellie, J. E. Harrison, M. L., Pike, L. J., Hellstrom, K. E., and Krebs, E. G. (1982) Proc. Natl. Acad. Sci. U. S. A. 79, 282-286). In order to determine if this protein was related to pp60src, the transformation-specific protein from Rous sarcoma virus, partial proteolysis maps of in vitro 32P-labeled pp58 and pp60src were prepared using Staphylococcus aureus V8 protease and papain. The maps were clearly different, indicating the pp58 is distinct from pp60src. However characterization of the tryptic fragment containing the single site of in vitro tyrosine phosphorylation in pp58 has revealed that the amino acid sequence around this site is extremely homologous to, if not identical with the sequence around the site of tyrosine phosphorylation in pp60src.

摘要

淋巴瘤细胞系LSTRA微粒部分中一种酪氨酸蛋白激酶的主要体外底物是一种分子量为58,000的蛋白质（pp58）（卡斯内利，J. E.；哈里森，M. L.；派克，L. J.；赫尔斯特伦，K. E.；以及克雷布斯，E. G.（1982年）《美国国家科学院院刊》79，282 - 286）。为了确定该蛋白质是否与劳斯肉瘤病毒的转化特异性蛋白pp60src相关，使用金黄色葡萄球菌V8蛋白酶和木瓜蛋白酶制备了体外32P标记的pp58和pp60src的部分蛋白酶解图谱。这些图谱明显不同，表明pp58与pp60src不同。然而，对包含pp58体外酪氨酸磷酸化单一位点的胰蛋白酶片段的表征显示，该位点周围的氨基酸序列即使与pp60src酪氨酸磷酸化位点周围的序列不完全相同，也极其同源。