摘要
纯化的大豆胰蛋白酶抑制剂Ｔｉａ和Ｔｉｂ分别经烷基化、ＣＮＢｒ裂解、普通ＰＡＧＥ电泳、Ｔｒｉｃｉｎｅ／ＳＤＳ－ＰＡＧＥ电泳分析，初步证明Ｔｉｄ的突变位点发生在蛋白Ｎ端１～８４氨基酸残基上．
Soybean seed storage proteins,Tia and Tid, were extracted and purified from corresponding cultivars. The proteins were subjected to alkylation, CNBr hydrolysis, polyacrylamide gel electrophoresis (PAGE) and Tricine/SDS-PAGE analysis. The mutation position was identified and was found to be located on a 9. 8 ku fragment,which corresponded to 1 ~84 amino acids of the protein.
出处
《复旦学报（自然科学版）》
CAS
CSCD
北大核心
1998年第2期229-232,共4页
Journal of Fudan University：Natural Science
基金
国家自然科学基金
关键词
大豆
胰蛋白酶抑制剂
突变位点
SBTi-A2
trypsin inhibitor of soybean
CNBr hydrolysis
mutation site
electrophoresis
