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pp60src酪氨酸激酶的底物p36与从牛主动脉中分离出的一种67 kDa蛋白质之间的序列同源性。

Sequence homologies between p36, the substrate of pp60src tyrosine kinase and a 67 kDa protein isolated from bovine aorta.

作者信息

Martin F, Derancourt J, Capony J P, Colote S, Cavadore J C

出版信息

Biochem Biophys Res Commun. 1987 Jun 15;145(2):961-8. doi: 10.1016/0006-291x(87)91059-x.

Abstract

A 67 kDa actin-binding protein was isolated from bovine aorta. Partial amino acid sequence determination of two large thermolysin peptides were used to compare 67 kDa bovine aorta protein and p36 the substrate of pp60src tyrosine kinase. Sequence analysis shows that 67 kDa bovine aorta protein shares common domains with p36 and possesses the consensus aminoacid sequences of mammalian Ca2+-dependent membrane-binding protein and p36/gelsolin.

摘要

从牛主动脉中分离出一种67 kDa的肌动蛋白结合蛋白。通过对两个大的嗜热菌蛋白酶肽段进行部分氨基酸序列测定,来比较67 kDa的牛主动脉蛋白和pp60src酪氨酸激酶的底物p36。序列分析表明,67 kDa的牛主动脉蛋白与p36具有共同的结构域,并且拥有哺乳动物钙依赖性膜结合蛋白和p36/凝溶胶蛋白的共有氨基酸序列。

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