The glycan structure of albumin Redhill, a glycosylated variant of human serum albumin

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• 作者：Kragh-Hansen ; Ulrich ; Donaldson ; David ; Jensen ; Poul Henning
• 关键词：Human serum albumin ; Genetic variant ; Glycoprotein ; N-Linked oligosaccharide ; Biantennary glycan ; Sialic acid ; Alb ; human serum albumin ; Alb A ; normal (wild-type) albumin ; Arg-Alb ; Alb A possessing an extra Arg at the N-terminus
• 刊名：Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
• 出版年：2001
• 出版时间：November 26, 2001
• 年：2001
• 卷：1550
• 期：1
• 页码：20-26
• 全文大小：221 K

文摘

Although human serum albumin is synthesized without carbohydrate, glycosylated variants of the protein can be found. We have determined the structure of the glycan bound to the double-mutant albumin Redhill (−1 Arg, 320 Ala→Thr). The oligosaccharide was released from the protein using anhydrous hydrazine, and its structure was investigated using neuraminidase and a reagent array analysis method, which is based on the use of specific exoglycosidases. The glycan was shown to be a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn. However, a minor part (11 mol % ) of the glycan was without sialic acid. The structure is principally the same as that of glycans bound to two other types of glycosylated albumin variants. Glycosylation can affect, for example, the fatty acid binding properties of albumin. Taking the present information into account, it is apparent that different effects on binding are caused not by different glycan structures but by different locations of attachment, with the possible addition of local conformational changes in the protein molecule.