牙龈卟啉菌381胞外膜泡中胰酶样蛋白酶的理化性质测定  

Characterization of trypsin-like protease(TLP)purificated from extracellular vesicles(ECV) of P.gingivalis 381

作　　者：倪龙兴[1] 史俊南[1] 陈镔复[1] 刘智广[1] 

机构地区：[1]西安市第四军医大学口腔医学院,西安市第四军医大学中心实验室

出　　处：《牙体牙髓牙周病学杂志》1995年第3期138-140,共3页Chinese Journal of Conservative Dentistry

摘　　要：对牙龈卟啉菌（Ｐｇ）３８１胞外膜泡中提取的胰酶样蛋白酶（ＴＬＰ）的理化性质进行了检测，结果表明：ＴＬＰ属于半胱氨酸类蛋白酶，分子量在天然状态时是４７６００ｕ，在ＳＤＳ－ＰＡＧＥ中为２８３００ｕ，表明它是由一个２８３００ｕ的亚基和一个或几个小于１００００ｕ的亚基组成；在ｐＨ７．５时，它的酶活性最高。The TLP(i.e.Gingivain) was purified from ECV of P. gingivalis 381 was active against benzoyl-L-arginine-ρ-nitroanilide and activated by thiol-containing agents and slightly inhibited by trypsin inhibitor.The molecular weights of the TLP were about 48500u by HPLC,and 11000u by SDS-PAGE.The maximum activity of the TLP were found at PH7.5.The results showed that.the TLP purified might belong to cysteine proteinase and might be polypeptidase which might be degraded by SDS and high temperature (100℃).

关 键 词：牙龈卟啉菌 胰酶样蛋白酶 理化特性 口腔细菌学 

分 类 号：R780.2[医药卫生—口腔医学]