对伴刀豆球蛋白A具有不同亲和力的α-蛋白酶抑制剂分子变体中聚糖的均匀性。

Uniformity of glycans within molecular variants of alpha-protease inhibitor with distinct affinity for concanavalin A.

作者信息

Bayard B, Kerckaert J P, Laine A, Hayem A

出版信息

Eur J Biochem. 1982 May 17;124(2):371-6. doi: 10.1111/j.1432-1033.1982.tb06602.x.

DOI:10.1111/j.1432-1033.1982.tb06602.x

Abstract

Human alpha 1-protease inhibitor contains four asparagine-linked carbohydrate chains per molecule. Three types of carbohydrate chains were released from the polypeptide backbone by hydrazinolysis: (a) biantennary (80%), (b) biantennary with an intercalated N-acetylglucosamine residue (14%), and (c) triantennary (6%). Using concanavalin-A-affinity chromatography, native and S-carboxymethylated alpha 1--protease inhibitor were fractionated into three distinct molecular variants which were shown to contain only one type (a, b, or c, respectively) of glycan per molecule. This and previous observations on other serum glycoproteins support the proposal of uniformity of glycan type within individual molecular variants of glycoproteins.

摘要

人α1-蛋白酶抑制剂每个分子含有四条天冬酰胺连接的碳水化合物链。通过肼解从多肽主链释放出三种类型的碳水化合物链：(a) 双天线型（80%），(b) 带有插入的N-乙酰葡糖胺残基的双天线型（14%），以及 (c) 三天线型（6%）。使用伴刀豆球蛋白A亲和色谱法，天然的和S-羧甲基化的α1-蛋白酶抑制剂被分离成三种不同的分子变体，这些变体显示每个分子仅含有一种类型（分别为a、b或c）的聚糖。这一结果以及之前对其他血清糖蛋白的观察结果支持了糖蛋白单个分子变体中聚糖类型具有一致性的提议。