Title : Effects of inhibitors of N-linked oligosaccharide processing on the secretion, stability, and activity of lecithin:cholesterol acyltransferase.

Pub. Date : 1991 Apr 2

PMID : 1901219






5 Functional Relationships(s)
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1 The structure and function of the carbohydrate moiety of human lecithin:cholesterol acyltransferase (LCAT) were determined by using several glycosidases in reaction with the isolated plasma protein or by using specific inhibitors of glycoprotein assembly with cultured cells secreting LCAT activity. Carbohydrates lecithin-cholesterol acyltransferase Homo sapiens
2 The structure and function of the carbohydrate moiety of human lecithin:cholesterol acyltransferase (LCAT) were determined by using several glycosidases in reaction with the isolated plasma protein or by using specific inhibitors of glycoprotein assembly with cultured cells secreting LCAT activity. Carbohydrates lecithin-cholesterol acyltransferase Homo sapiens
3 The structure and function of the carbohydrate moiety of human lecithin:cholesterol acyltransferase (LCAT) were determined by using several glycosidases in reaction with the isolated plasma protein or by using specific inhibitors of glycoprotein assembly with cultured cells secreting LCAT activity. Carbohydrates lecithin-cholesterol acyltransferase Homo sapiens
4 Analysis of the plasma enzyme indicated that almost all of the large carbohydrate moiety of LCAT (approximately 25% w/w) was N-linked with part of the high-mannose and part of the complex type. Carbohydrates lecithin-cholesterol acyltransferase Homo sapiens
5 This analysis was confirmed with metabolic inhibitors of carbohydrate processing by using CHO cells stably transfected with the human LCAT gene. Carbohydrates lecithin-cholesterol acyltransferase Homo sapiens