HUMAN ERYTHROCYTE-MEMBRANE PROTEIN-4.2 IS PALMITOYLATED

被引:17
|
作者
DAS, AK [1 ]
BHATTACHARYA, R [1 ]
KUNDU, M [1 ]
CHAKRABARTI, P [1 ]
BASU, J [1 ]
机构
[1] BOSE INST, DEPT CHEM, Kolkata 700009, W BENGAL, INDIA
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1994年 / 224卷 / 02期
关键词
D O I
10.1111/j.1432-1033.1994.00575.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Protein 4.2 is a major protein of the human erythrocyte membrane. It has previously been shown to be N-myristoylated. After labeling of intact human erythrocytes with [H-3]palmitic acid, radioactivity was found to be associated with protein 4.2 by immunoprecipitation of peripheral membrane proteins extracted at pH 11 from ghosts with anti-(4.2) sera, followed by SDS/PAGE and fluorography. The fatty acid linked to protein 4.2 was identified as palmitic acid after hydrolysis of protein and thin-layer chromatography of the fatty acid extracted in the organic phase. Protein 4.2 could be depalmitoylated with hydroxylamine, suggesting a thioester linkage. Depalmitoylated protein 4.2 showed significantly decreased binding to protein-4.2-depleted membranes, compared to native protein 4.2.
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页码:575 / 580
页数:6
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