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莱氏无胆甾原体中的酰化蛋白。

Acylated proteins in Acholeplasma laidlawii.

作者信息

Dahl C E, Sacktor N C, Dahl J S

出版信息

J Bacteriol. 1985 Apr;162(1):445-7. doi: 10.1128/jb.162.1.445-447.1985.

DOI:10.1128/jb.162.1.445-447.1985
PMID:3980443
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC219011/
Abstract

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.

摘要

通过对放射性标记膜进行一维凝胶电泳，在两株莱氏无胆甾原体中测定了长链脂肪酸对膜蛋白的共价修饰。在检测到的50多种膜多肽中，约30种被[3H]棕榈酸标记，而未证实[3H]油酸与膜蛋白的共价结合。我们认为，在这些无壁细菌中，饱和脂肪酸对膜蛋白的酰化作用可能有助于确保膜的结构完整性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c157/219011/19c2f9742900/jbacter00221-0456-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c157/219011/832621a26345/jbacter00221-0456-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c157/219011/19c2f9742900/jbacter00221-0456-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c157/219011/832621a26345/jbacter00221-0456-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c157/219011/19c2f9742900/jbacter00221-0456-b.jpg

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Acylated proteins in Acholeplasma laidlawii.莱氏无胆甾原体中的酰化蛋白。
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2
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