Kimura M, Kouzuma Y, Yamasaki N
Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.
Biosci Biotechnol Biochem. 1993 Jan;57(1):102-6. doi: 10.1271/bbb.57.102.
The amino acids of the chymotrypsin inhibitor (ECI) from the Erythrina variegata seeds have been sequenced. The sequence was solved by analysis of peptides derived from the protein by enzymatic digestions with trypsin and Staphylococcus aureus V8 proteinase, as well as by chemical cleavage with o-iodosobenzoic acid. The ECI consists of 179 amino acid residues with a pyroglutamic acid as the N-terminal residue and has a calculated molecular weight of 19,791. Comparison of this sequence with the sequences of the two trypsin inhibitors, ETIa and ETIb, from the E. variegata seeds shows that about 60% of the residues of ECI are identical to those of ETIa and ETIb and that the reactive sites, Arg63, in ETIa and ETIb change to Leu64 in ECI.
已对刺桐种子中胰凝乳蛋白酶抑制剂（ECI）的氨基酸进行了测序。该序列通过对用胰蛋白酶和金黄色葡萄球菌V8蛋白酶进行酶切以及用邻碘苯甲酸进行化学裂解从蛋白质中得到的肽段进行分析得以解析。ECI由179个氨基酸残基组成，N端残基为焦谷氨酸，计算分子量为19,791。将该序列与刺桐种子中的两种胰蛋白酶抑制剂ETIa和ETIb的序列进行比较，结果表明ECI约60%的残基与ETIa和ETIb的残基相同，并且ETIa和ETIb中的活性位点Arg63在ECI中变为Leu64。
