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Structure of malhamensilipin A, an inhibitor of protein tyrosine kinase, from the cultured chrysophyte Poterioochromonas malhamensis.

作者信息

Chen J L, Proteau P J, Roberts M A, Gerwick W H, Slate D L, Lee R H

机构信息

College of Pharmacy, Oregon State University, Corvallis 97331.

出版信息

J Nat Prod. 1994 Apr;57(4):524-7. doi: 10.1021/np50106a015.

Abstract

A new chlorosulfolipid, malhamensilpin A [1] was isolated from the cultured chrysophyte Poterioochromonas malhamensis. Malhamensilipin A was demonstrated to be a modest inhibitor of pp60v-src protein tyrosine kinase. The structure was determined by detailed spectral analysis to be a novel C24 hexachloro lipid containing a vinyl sulfate ester (2,11,12,13,15,16-hexachloro-14-hydroxy-n-tetracos-1E-enol-1-sulfa te).

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