无黄无胆甾原体中的卵黄高磷蛋白激酶活性。

Phosvitin kinase activity in Acholeplasma axanthum.

作者信息

Platt M W, Rottem S

机构信息

Department of Membrane and Ultrastructure Research, Hebrew University-Hadassah Medical School, Jerusalem, Israel.

出版信息

FEBS Lett. 1988 Dec 19;242(1):97-100. doi: 10.1016/0014-5793(88)80993-1.

DOI:10.1016/0014-5793(88)80993-1

PMID:3203746

Abstract

Incubating the soluble fraction derived from A. axanthum with phosvitin and [gamma-32P]ATP results in the phosphorylation of phosvitin. Casein, histone and kemptide were practically ineffective substrates, whereas a 55 kDa protein of M. gallisepticum was efficiently phosphorylated. The enzymatic activity has an optimal pH in the pH range 6.0-6.2 and requires divalent cations. The activity was inhibited by ammonium sulfate, heparin and sulphydryl blocking reagents, but was not affected by calmodulin with or without Ca2+ or by cyclic AMP.

摘要

将来自黄眼草的可溶性组分与卵黄高磷蛋白及[γ-32P]ATP一起温育会导致卵黄高磷蛋白发生磷酸化。酪蛋白、组蛋白和肯普肽实际上不是有效的底物，而鸡败血支原体的一种55 kDa蛋白质能被高效磷酸化。该酶活性在pH 6.0 - 6.2范围内有最佳pH值，并且需要二价阳离子。其活性受到硫酸铵、肝素和巯基封闭试剂的抑制，但不受有或没有Ca2+的钙调蛋白或环磷酸腺苷的影响。