| Literature DB >> 7925374 |
A K Das1, R Bhattacharya, M Kundu, P Chakrabarti, J Basu.
Abstract
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 [3H]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.Entities:
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Year: 1994 PMID: 7925374 DOI: 10.1111/j.1432-1033.1994.00575.x
Source DB: PubMed Journal: Eur J Biochem ISSN: 0014-2956