Premium
Fatty acid acylation of membrane skeletal proteins in human erythrocytes
Author(s) -
Maretzki Dieter,
Mariani Mariagabriella,
Lutz Hans U.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80033-f
Subject(s) - acylation , erythrocyte membrane , chemistry , biochemistry , fatty acid , membrane , catalysis
Fatty acid acylation of membrane proteins was studied on human erythrocytes by measuring incorporation of [ 3 H]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 [ 3 H]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 aeylated 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 uran along with a small subpopulation of spectrin which was also tightly associated with the membrane.