Acylated proteins in Acholeplasma laidlawii.
AUTOR(ES)
Dahl, C E
RESUMO
The covalent modification of membrane proteins by long-chain fatty acids was determined in two strains of Acholeplasma laidlawii by one-dimensional gel electrophoresis of radiolabeled membranes. Of the more than 50 membrane polypeptides detected, approximately 30 were labeled with [3H]palmitate, whereas covalent binding of [3H]oleate to membrane proteins could not be demonstrated. We suggest that in these wall-less bacteria, membrane protein acylation with saturated fatty acids may serve to ensure the structural integrity of the membrane.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=219011Documentos Relacionados
- Adenylate energy charge in Acholeplasma laidlawii.
- Cytoplasmic helical structure associated with Acholeplasma laidlawii.
- Membrane composition and virus susceptibility of Acholeplasma laidlawii.
- Nucleotide sequence of tryptophan tRNA gene in Acholeplasma laidlawii.
- Immunological properties of glycolipids from membranes of Acholeplasma laidlawii.
