荞麦种子中两种胰蛋白酶抑制剂的完整氨基酸序列。

Complete amino acid sequences of two trypsin inhibitors from buckwheat seed.

作者信息

Pandya M J, Smith D A, Yarwood A, Gilroy J, Richardson M

机构信息

IACR-Long Ashton Research Station, Department of Agricultural Sciences, University of Bristol, U.K.

出版信息

Phytochemistry. 1996 Sep;43(2):327-31. doi: 10.1016/0031-9422(96)00311-1.

DOI:10.1016/0031-9422(96)00311-1

PMID:8862028

Abstract

The major trypsin isoinhibitors from seed extracts of buckwheat (Fagopyrum esculentum Mönch) were purified by affinity chromatography, anion exchange chromatography, anion exchange HPLC and reversed-phase HPLC, and the complete amino acid sequences of two isoinhibitors, BTI-1 and BTI-2, were established by automated Edman degradation. Each isoinhibitor consists of a single polypeptide chain of 69 amino acids, including two Cys residues. The N-terminal sequence of a third isoform, BTI-3, was also determined. The buckwheat trypsin isoinhibitors exhibit clear sequence similarities with the potato chymotrypsin inhibitor I family of serine proteinase inhibitors.

摘要

从荞麦（苦荞麦）种子提取物中分离出的主要胰蛋白酶抑制剂，通过亲和色谱、阴离子交换色谱、阴离子交换高效液相色谱和反相高效液相色谱进行纯化，并通过自动埃德曼降解法确定了两种抑制剂BTI-1和BTI-2的完整氨基酸序列。每种抑制剂均由一条含69个氨基酸的单多肽链组成，其中包括两个半胱氨酸残基。还测定了第三种异构体BTI-3的N端序列。荞麦胰蛋白酶抑制剂与丝氨酸蛋白酶抑制剂的马铃薯胰凝乳蛋白酶抑制剂I家族具有明显的序列相似性。