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Membrane‐binding sites for acyl carrier protein in Escherichia coli
Author(s) -
Bayan Nicolas,
Therisod Helene
Publication year - 1989
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(89)80963-9
Subject(s) - dissociation constant , escherichia coli , biochemistry , binding site , membrane protein , bacterial outer membrane , membrane , chemistry , binding protein , phospholipid , protein–lipid interaction , biophysics , enzyme , vesicle associated membrane protein 8 , biology , integral membrane protein , receptor , gene
We report that membrane vesicles of Escherichia coli contain protein‐binding sites for acyl carrier protein. Scatchard analysis of the binding indicates a dissociation constant around 0.35 μM and a maximum number of protein‐binding sites around 50 pmol per mg of membrane protein. Binding is on the inner membrane while the outer membrane is devoid of binding sites. These results are consistent with the fact that some acyl carrier protein‐dependent enzymes implicated in phospholipid‐ and membrane‐derived oligosaccharide biosynthesis are localized in the cytoplasmic membrane.

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