磷酸肌醇与髓鞘碱性蛋白的共价连接：[32P]磷酸肌醇在体外掺入髓鞘碱性蛋白。

Covalent linkage of phosphoinositides to myelin basic protein: in vitro incorporation of [32P] phosphoinositides to myelin basic protein.

作者信息

Chiu K C, Smith R A

出版信息

Biochem Biophys Res Commun. 1987 Jun 15;145(2):803-9. doi: 10.1016/0006-291x(87)91036-9.

Abstract

We have previously reported that the covalent attachment of phosphoinositides to myelin basic protein (MBP) occurs both in vivo and in vitro [Smith, R. A. et al. (1986) Biochemistry 25:2677-2681; Biochemistry 25:2682-2686; and Biochem. Biophys. Res. Comm. 316:426-432]. Phosphoinositidation of MBP was also detected when [32P] phosphoinositides were incubated with myelin pretreated with Triton X-100 and EGTA. Less than 10% of this covalent linkage of phosphoinositides to MBP survived after acidic treatment (0.1 N HCl at 37 degrees C for 10 min). MBP is predicted to lack sufficient hydrophobicity to bind to membranes as shown by analysis of its amino acid sequence for hydrophobic regions and thus its phosphoinositidation may provide an anchor for this purpose.

摘要

我们之前曾报道过，磷酸肌醇与髓鞘碱性蛋白（MBP）的共价连接在体内和体外均会发生[史密斯，R.A.等人（1986年）《生物化学》25:2677 - 2681；《生物化学》25:2682 - 2686；以及《生物化学与生物物理研究通讯》316:426 - 432]。当[³²P]磷酸肌醇与用 Triton X - 100 和 EGTA 预处理的髓鞘一起孵育时，也检测到了 MBP 的磷酸肌醇化。在酸性处理（37℃下用 0.1 N HCl 处理 10 分钟）后，这种磷酸肌醇与 MBP 的共价连接中存活下来的不到 10%。通过对其氨基酸序列的疏水区分析表明，预计 MBP 缺乏足够的疏水性来结合到膜上，因此其磷酸肌醇化可能为此提供一个锚定作用。