作者: Rodolfo A. UGALDE , Roberto J. STANELONI , Luis F. LELOIR
DOI: 10.1111/J.1432-1033.1980.TB06144.X
关键词:
摘要: Further work on microsomal glucosidases of rat liver has confirmed that at least two enzymes are involved in the removal glucose from glucose-containing oligosaccharide. One acts oligosaccharide containing three residues and another which one or glucoses. The glucosidase (Glc)2(Man)9(GlcNAc)2 could be purified with a ConcanavalinA—Sepharose column followed by electrofocusing. This preparation was active glucoses. Heat inactivation inhibition disaccharides parallel for both activities. Inhibition (Glc)3(Man)9(GlcNAc)2 obtained kojibiose an α 1–2 linkage, while acting (Glc)1–2(Man)9-(GlcNAc)2 inhibited nigerose (α 1–3 linkage), maltose 1–4 linkage) higher concentration. None β anomers inhibited. These results consistent configuration glucoses dolichyl-dinhosphate-linked Kojibiose found to inhibit action not only free but also protein-bound one.