2.3.1.43	glycoprotein	-	487028, 661231, 757930	
2.3.1.43	glycoprotein	13% hexoses, 6.2% hexosamines	486985	
2.3.1.43	glycoprotein	21% w/w carbohydrate, including hexoses, hexosamines and sialic acids	486989, 486991	
2.3.1.43	glycoprotein	24% carbohydrate by weight, 13 mol of mannose, 30 mol of galactose, 17 mol of glucosamine and 13 mol of sialic acid per mol of enzyme protein	486978, 487007	
2.3.1.43	glycoprotein	25% carbohydrate	486981, 486985	
2.3.1.43	glycoprotein	a recombinant C-terminal histidine tagged enzyme has similar carbohydrate moieties than the enzyme purified from plasma	487023	
2.3.1.43	glycoprotein	almost all of the carbohydrate moiety of LCAT is N-linked with part of the high-mannose and part of the complex type	486988	
2.3.1.43	glycoprotein	almost all of the N-linked glycans in human LCAT are fucosylated and sialylated. The predominant LCAT N-linked glycoforms are biantennary glycans, followed by triantennary sugars, whereas the level of tetraantennary glycans is much lower. Glycans at the Fc N-linked site exclusively contain typical asialobiantennary structures. Recombinant human lecithin-cholesterol acyltransferase Fc fusion chimeric protein is also confirmed to have mucin-type glycans attached at T407 and S409. When LCAT-Fc fusions are constructed using a G-S-G-G-G-G linker, an unexpected 1632 Da xylose-based glycosaminoglycan (GAG) tetrasaccharide core of Xyl-Gal-Gal-GlcA is attached to S418. Several minor intermediate species including Xyl, Xyl-Gal, Xyl-Gal-Gal, and a phosphorylated GAG core are also present. E416 (the C-terminus of LCAT) combined with the linker sequence is likely serving as a substrate for peptide O-xylosyltransferase	737203	
2.3.1.43	glycoprotein	analysis of glycosylation pattern, glycosylation e.g. at residues Asn20, Asn84, and Asn272, modification of the glycan side chains by use of drugs and by other enzymes, physiological function, glycosylation pattern of the recombinant enzymes differs from the wild-type, overview	661432	
2.3.1.43	glycoprotein	analysis of sugar composition, overview	663302	
2.3.1.43	glycoprotein	four N-glycosydation and two O-glycosylation sites attached to glycans	487010	
2.3.1.43	glycoprotein	glycans in recombinant enzyme, expressed in baby hamster kidney cells, have bi- and triantennary structures with or without core fucosylation	487022	
2.3.1.43	glycoprotein	glycans structure determined by mass spectrometry and linkage analysis	487022	
2.3.1.43	glycoprotein	glycosylation in a recombinant enzyme is more extensive than that of isolated from plasma	487024	
2.3.1.43	glycoprotein	human enzyme cloned in animal cells has different degree of glycosydation	487010	
2.3.1.43	glycoprotein	recombinant enzyme expressed in hepatic Mc-7777 cells has biantennary structure oligosaccharide moieties	487014	
2.3.1.43	glycoprotein	removal of individual carbohydrate chains affects activity	487010	
2.3.1.43	glycoprotein	the enzyme exists as a family of molecular species having a common core polypeptide with the number of sialic acid residues varying from 10 to 16	486999	
2.3.1.43	glycoprotein	the enzyme is highly glycosylated with four potential N-linked glycosylation sites and two putative O-linked sites	737191	
2.3.1.43	glycoprotein	with a 5% sialic acid content	486981, 486985