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大豆(G.max)胰蛋白酶抑制剂SBTi-A_2新类型Ti~x的纯化及其性质研究
引用本文:严晴燕,曹凯鸣,徐隽,林锐,李严,顾其敏,赵述文.大豆(G.max)胰蛋白酶抑制剂SBTi-A_2新类型Ti~x的纯化及其性质研究[J].复旦学报(自然科学版),1996(2).
作者姓名:严晴燕  曹凯鸣  徐隽  林锐  李严  顾其敏  赵述文
作者单位:复旦大学,云南大学,吉林省农业科学院
摘    要:用丙酮脱脂、稀酸处理、硫酸铵盐析和DEAE-52纤维素柱层析等方法从大豆(G.max)中分离纯化得一种新类型胰蛋白酶抑制剂Tix.SDS-PAGE分析显示Tix与已知的大豆蛋白酶抑制剂Tia的相对分子质量均为21000,且N-末端均为AsP;亲和电泳分析显示Tix与Tia均可与胰蛋白酶完全结合;BAEE法测定显示出Tix对胰蛋白酶活性的抑制略小于Tia;两者经CNBr裂解后电泳分析得到相同带型;纯化样品的氨基酸组成分析显示Tix比Tia多了两个碱性氨基酸,因而Tix带有更多的正电荷.研究结果初步证明Tix是Kunitz类型中一种新的胰蛋白酶抑制剂.

关 键 词:大豆  胰蛋白酶抑制剂  纯化  性质

Purification and characterization of a new electrophoretic variant of SBTi-A_2 from soybean(G. max) seed storage protein
Yan Qingyan, Cao Kaiming, Xu Jun, Lin Rui, Li Yan, Gu Qimin.Purification and characterization of a new electrophoretic variant of SBTi-A_2 from soybean(G. max) seed storage protein[J].Journal of Fudan University(Natural Science),1996(2).
Authors:Yan Qingyan  Cao Kaiming  Xu Jun  Lin Rui  Li Yan  Gu Qimin
Abstract:ia and Tix were extracted from soybean seeds following the method modified by Mihoko Yamanoto, and purified by DEAE-52 column. Tix was the same relative molecular mass and N-terminal residue as Tia. Both inhibited trypsin activity at a ratio of 1: 1,but K, value of Tix was slightly higher than that of Tia. The results of PAGE and HPLC showed that the CNBr fragments of Tix were similar to those of Tia.In amino acid composition,there were two residues differences between Tix and Tia, with the result that Tix was more positively charged than Tia. Tix is a new electrophoretic variant of SBTi-A2 from soybean seed storage protein.
Keywords:soybean(G  max)  trypsin inhibitor  purification  property
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