Belozersky M A, Dunaevsky Y E, Musolyamov A K, Egorov T A
AN Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russian Federation.
IUBMB Life. 2000 Apr;49(4):273-6. doi: 10.1080/15216540050033122.
The complete amino acid sequence of protease inhibitor BWI-4a from buckwheat (Fagopyrum esculentum Moench) seeds, consisting of 67 amino acid residues with a single disulfide bond, has been established by Edman degradation in combination with matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Its N terminus is blocked by a pyroglutamic acid residue. Mass spectrometric analysis revealed that inhibitor BWI-4a is present in buckwheat seeds in two isoforms with a single amino acid substitution of Ala40 for Gly40. The reactive site of the inhibitor contains an Arg43-Asp44 bond. Analysis of the amino acid sequence suggests that the buckwheat seed protease inhibitor is a member of the potato proteinase inhibitor I family.
已通过埃德曼降解法结合基质辅助激光解吸电离飞行时间质谱法确定了来自荞麦（苦荞麦）种子的蛋白酶抑制剂BWI-4a的完整氨基酸序列，该序列由67个氨基酸残基组成，含有一个二硫键。其N端被一个焦谷氨酸残基封闭。质谱分析表明，抑制剂BWI-4a在荞麦种子中以两种同工型存在，其中Ala40被Gly40单氨基酸取代。该抑制剂的活性位点包含一个Arg43-Asp44键。氨基酸序列分析表明，荞麦种子蛋白酶抑制剂是马铃薯蛋白酶抑制剂I家族的成员。
