人类红细胞膜骨架蛋白的脂肪酸酰化作用

Fatty acid acylation of membrane skeletal proteins in human erythrocytes.

作者信息

Maretzki D, Mariani M, Lutz H U

机构信息

Laboratory for Biochemistry, Swiss Federal Institute of Technology, Zurich.

出版信息

FEBS Lett. 1990 Jan 1;259(2):305-10. doi: 10.1016/0014-5793(90)80033-f.

DOI:10.1016/0014-5793(90)80033-f

PMID:2294020

Abstract

Fatty acid acylation of membrane proteins was studied on human erythrocytes by measuring incorporation of [3H]palmitate at different specific radioactivities. A 55 kDa polypeptide within the band 4.5 region was the main acceptor protein for acylation by fatty acids (palmitate, stearate, oleate), while other polypeptides (80, 65, 48, 30 kDa) incorporated [3H]palmitate slowly, in substoichiometric amounts. Integral membrane proteins were preferentially fatty acid acylated. Skeletal membrane proteins were, however, poorly labeled. Neither purified ankyrin nor band 4.1 protein were fatty acid acylated in human erythrocytes. On the other hand, label associated with high molecular weight skeletal proteins resisted low and high ionic strength extractions, and was extracted selectively by urea [corrected] along with a small subpopulation of spectrin which was also tightly associated with the membrane.

摘要

通过测量不同比活度的[3H]棕榈酸酯的掺入情况，对人红细胞膜蛋白的脂肪酸酰化进行了研究。4.5区带内的一种55 kDa多肽是脂肪酸（棕榈酸酯、硬脂酸酯、油酸酯）酰化的主要受体蛋白，而其他多肽（80、65、48、30 kDa）以亚化学计量的量缓慢掺入[3H]棕榈酸酯。整合膜蛋白优先被脂肪酸酰化。然而，骨架膜蛋白的标记很差。在人红细胞中，纯化的锚蛋白和带4.1蛋白都没有被脂肪酸酰化。另一方面，与高分子量骨架蛋白相关的标记物抵抗低离子强度和高离子强度的提取，并与一小部分也与膜紧密结合的血影蛋白一起被尿素选择性提取[校正后]。