猪血浆巯基蛋白酶抑制剂的分离纯化及性质研究  

PURIFICATION AND CHARACTERIZATION OF A SULFHYDRYL PROTEASE INHIBITOR FROM PORCINE PLASMA

作　　者：郑常文[1] 董长江[1] 唐宏力[1] 李湘萍[2] 郑念新 

机构地区：[1]四川大学生物技术研究中心 [2]广西大学 [3]成都体育学院运动医学系

出　　处：《四川大学学报（自然科学版）》1993年第3期392-398,共7页Journal of Sichuan University(Natural Science Edition)

摘　　要：用(NH_4)_2SO_4分段盐析,DEAE-纤维素离子交换和Papain—Sepharose亲和层析,从猪血浆纯化了一种巯基蛋白酶抑制剂(SUlfhydryl proteinase inhibitor;简称SPI);纯化倍数为54.36倍.经高pH、低PH不连续电泳呈一条区带.含糖量为7.77％;PI为4.80.氨基酸组成分析表明,猪血SPI富含酸性氨基酸、芳香族氨基酸和含硫氨基酸.用SDS-PAGE和SephadexG-100层析,测得分子量为130000d和131000d,由两个分子量略有差别的亚基组成.对木瓜蛋白酶有强烈抑制作用,对胰蛋白酶无作用。α-螺旋结构含量高。A porcine plasma protease inhibitor specific for sulfhydryl protease was successfully purified by (NH4)2SO4 fraction precipitation, DEAE-cellulose chromatography and papain-Sepharose affinity chromatography. The purification fold is 54. 36. The SPI is a glycoprotein,containing 7. 77% carbohydrate, the molecular weight is 131000 dalton, consisting of two identical subunit. The PI is 4. 8. Amino acid analyses of the purified SPI shows there is a large amount of acidic amino acids, aromatic amino acids and sulphureous amino acid. It inhibits papin strengly but almost has no effect on trypsin. It shows a high a-helix structure.

关 键 词：猪 血浆 巯基蛋白酶 抑制剂 

分 类 号：Q553[生物学—生物化学]