Role of sialic acid residues in crossed immuno‐affinoelectrophoresis of α1‐proteinase inhibitor

FEBS Letters

Franc, J.L.²  Mallet, B.¹  Zattara, M.C.¹ 

[1] Laboratoire de Chimie Biologique, Faculté de Médecine, 27, BdJean Moulin, 13385 Marseille Cédex 05, France;Unité Associée 178 CNRS, Unité 38INSERM, Faculté de Médecine, 27, Bd Jean Moulin, 13385 Marseille Cédex 05, France

关键词: Crossed immuno-affinoelectrophoresis;    Sialic acid;    α1-Proteinase inhibitor;    N-glycan;    Concanavalin A;   

DOI  :  10.1016/0014-5793(90)80147-B

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have investigated the importance of the degree of sialylation when an acute phase glycoprotein, α₁-proteinase inhibitor (α₁-Pi), was analysed both by affinity chromatography on concanavalin A (Con A)-Sepharose and by crossed immuno-affinoelectrophoresis (CIAE) using Con A in the first dimension. Human α₁-Pi was isolated by immunosorption chromatography and then more or less desialylated. On Con A-Sepharose chromatography no significant difference was observed in the percentage of the two fractions (retained or not retained) whatever the degree of desialylation. In contrast by CIAE this degree was largely involved in the separation of the different isoforms obtained in the first dimension.

【 授权许可】

Unknown