endo-beta-N-acetylglucosaminidase F: endoglycosidase from Flavobacterium meningosepticum that cleaves both high-mannose and complex glycoproteins.

摘要: Abstract We have detected an endoglycosidase activity produced by Flavobacterium meningosepticum. This enzyme, named endo F, cleaves glycans of both the high-mannose and complex type linked through asparagine to protein backbone. The data indicate that cleavage occurs via hydrolysis glycosidic bond N,N'-diacetylchitobiose core structure adjacent asparagine, similar due H D. Extreme variability was noted in availability this site among N-linked glycoproteins. Glycoproteins retrovirus, lymphocytic choriomeningitis virus, Pichinde HLA-A -B antigens were readily cleaved presence nonionic detergent. Others, such as ovalbumin, fetuin, bromelain, ovomucoid, alpha 1-acid glycoprotein, immunoglobulin G, influenza virus hemagglutinin became susceptible only after reduction alkylation or when performed 1% 2-mercaptoethanol. Endo F should prove useful study backbones discrete entities for defining nature glycan-protein interface.