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