Journal article
Relationship of the structure and biological activity of the natural homologues of tunicamycin
Journal of Biological Chemistry, Vol.257(6), pp.3105-3109
25/Mar/1982
Abstract
The antibiotic tunicamycin was separated into 16 different components using reversed-phase high performance liquid chromatography. The effect of the eight major tunicamycin homologues on protein glycosylation and protein biosynthesis was examined. All homologues tested inhibited lipid-mediated protein glycosylation in chick or mouse fibroblasts. These homologues also inhibited the transfer of N-acetylglucosamine-1-phosphate from UDP-N-acetylglucosamine to dolichyl phosphate in chick liver microsome preparations, whereas the transfer of mannose from GDP-mannose to the lipid acceptor was hardly affected. The inhibition of protein glycosylation in fibroblasts or in microsomal preparations was concentration-dependent and maximum inhibition occurred at different concentrations for different homologues. The eight homologues differed in their ability to cause inhibition of protein synthesis.
Details
- Title
- Relationship of the structure and biological activity of the natural homologues of tunicamycin
- Creators
- D DUKSIN (null) - The Weizmann Institute of ScienceWC MAHONEY (null) - University of Washington
- Resource Type
- Journal article
- Publication Details
- Journal of Biological Chemistry, Vol.257(6), pp.3105-3109; 25/Mar/1982
- Number of pages
- 5
- Language
- English
- Grant note
- The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact
- Scientific Unit
- The Weizmann Institute of Science
- Record Identifier
- 993265703303596
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