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Enzymatic deglycosylation of bovine rhodopsin.

作者信息

Plantner J J, Le M L, Kean E L

机构信息

Department of Surgery, School of Medicine, Case Western Reserve University, Cleveland, OH 44106.

出版信息

Exp Eye Res. 1991 Aug;53(2):269-74. doi: 10.1016/0014-4835(91)90083-q.

DOI:10.1016/0014-4835(91)90083-q
PMID:1833217
Abstract

We have investigated the action of three endo N-acetylglucosaminidases on rhodopsin. The oligosaccharide chains of native and denatured opsin and rhodopsin, both solubilized and membrane-bound, were shown to be cleaved by endohexosaminidase H, endohexosaminidase F, and peptide-N-glycosidase F (PNGase F) as revealed by SDS-PAGE. These enzymes were shown to be free of protease activity. Under correct conditions, the endoglycosidases could release one or both carbohydrate chains. Rhodopsin and opsin at concentrations between 2 and 65 nmol ml-1 were cleaved, with more complete deglycosylation occurring at the higher concentrations.

摘要

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