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蚕豆凝集素favin的氨基酸序列及变异形式

Amino acid sequence and variant forms of favin, a lectin from Vicia faba.

作者信息

Hopp T P, Hemperly J J, Cunningham B A

出版信息

J Biol Chem. 1982 Apr 25;257(8):4473-83.

PMID:7068646
Abstract

We have determined the complete amino acid sequence (182 residues) of the beta chain of favin, the glucose-binding lectin from fava beans (Vicia faba), and have established that the carbohydrate moiety is attached to Asn 168. Together with the sequence of the alpha chain previously reported (Hemperly, J. J., Hopp, T. P., Becker, J. W., and Cunningham, B. A. (1979) J. Biol. Chem. 254, 6803-6810), these data complete the analysis of the primary structure of the lectin. We have also examined minor polypeptides that appear in all preparations of favin. Two lower molecular weight species (Mr = 9,500-11,600) appear to be fragments of the beta chain resulting from cleavage following Asn 76, whereas six high molecular weight forms (Mr = 25,000 or greater) appear to include aggregates of the beta chain and possibly some alternative products of chain processing.

摘要

我们已经确定了蚕豆(野豌豆)中葡萄糖结合凝集素蚕豆凝集素β链的完整氨基酸序列(182个残基),并确定碳水化合物部分连接在天冬酰胺168位上。连同先前报道的α链序列(亨珀利,J. J.,霍普,T. P.,贝克尔,J. W.,和坎宁安,B. A.(1979年)《生物化学杂志》254,6803 - 6810),这些数据完成了对该凝集素一级结构的分析。我们还研究了在所有蚕豆凝集素制剂中出现的次要多肽。两种较低分子量的物种(Mr = 9500 - 11600)似乎是β链在天冬酰胺76位之后裂解产生的片段,而六种较高分子量的形式(Mr = 25000或更大)似乎包括β链的聚集体以及可能的一些链加工替代产物。

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1
Amino acid sequence and variant forms of favin, a lectin from Vicia faba.蚕豆凝集素favin的氨基酸序列及变异形式
J Biol Chem. 1982 Apr 25;257(8):4473-83.
2
The chemical characterization of favin, a lectin isolated from Vicia faba.从蚕豆中分离出的凝集素——蚕豆凝集素的化学特性
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