| Autor: |
Das, Amit K., Bhattacharya, Raja, Kundu, Manikuntala, Chakrabarti, Parul, Basu, Joyoti |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; 9/1/94, Vol. 224 Issue 2, p575-580, 6p |
| Abstrakt: |
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 prorein 4.2 showed significantly decreased binding to protein-4.2-depleted membranes, compared to native protein 4.2. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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