无患子种子中的胰蛋白酶抑制剂：纯化、特性及对害虫消化酶的活性。
A trypsin inhibitor from Sapindus saponaria L. seeds: purification, characterization, and activity towards pest insect digestive enzyme.
机构信息
Laboratório de Purificação de Proteínas e suas Funções Biológicas, Departamento de Tecnologia de Alimentos e Saúde Pública, Centro de Ciências Biológicas e da Saúde, Universidade Federal do Mato Grosso do Sul (UFMS), Cidade Universitária S/N, Caixa Postal 549, Campo Grande, MS, CEP 79070-900, Brazil.
出版信息
Protein J. 2011 Jan;30(1):9-19. doi: 10.1007/s10930-010-9296-7.
The present paper describes the purification, characterization and determination of the partial primary structure of the first trypsin inhibitor isolated from the family Sapindaceae. A highly stable, potent trypsin inhibitor (SSTI) was purified to homogeneity. SDS-PAGE analysis revealed that the protein consists of a two-polypeptide chain with molecular masses of approximately 15 and 3 kDa. The purified inhibitor inhibited bovine trypsin at a 1:1 M ratio. Kinetic analysis revealed that the protein is a competitive inhibitor with an equilibrium dissociation constant of 10⁻⁹ M for trypsin. The partial NH₂- terminal sequence of 36 amino acids in SSTI indicates homology with other members of the trypsin-inhibitor family from different sources. This inhibitor is highly stable in the presence of denaturing agents. SSTI showed significant inhibitory activity against trypsin-like proteases present in the larval midgut on Anagasta kuehniella, Corcyra cephalonica, Diatreae saccharalis and Anticarsia gemmatalis.
本文描述了从无患子科中分离得到的第一种胰蛋白酶抑制剂的纯化、特性鉴定和部分一级结构测定。一种高度稳定、高效的胰蛋白酶抑制剂（SSTI）被纯化为均一状态。SDS-PAGE 分析表明，该蛋白由两条具有约 15 和 3 kDa 分子量的多肽链组成。纯化的抑制剂以 1:1 M 的比例抑制牛胰蛋白酶。动力学分析表明，该蛋白是一种竞争性抑制剂，对胰蛋白酶的平衡解离常数为 10⁻⁹ M。SSTI 的 36 个氨基酸的部分 NH₂-末端序列与来自不同来源的胰蛋白酶抑制剂家族的其他成员具有同源性。该抑制剂在变性剂存在下非常稳定。SSTI 对小菜蛾、玉米象、甜菜夜蛾和银纹夜蛾幼虫中肠存在的胰蛋白酶样蛋白酶表现出显著的抑制活性。
Zotero 插件