猪心苹果酸脱氢酶酶学性质及稳定性研究  

ENZYMATIC PROPERTIES AND STABIILITY OF MALATE DEHYDROGENASE FROM PORCINE HEART

作　　者：龚韧[1] 张大伟[1] 江龙法[1] 孙艳[1] 杨海麟[1] 王武[1] 

机构地区：[1]江南大学工业生物技术教育部重点实验室,江苏无锡214122

出　　处：《河南工业大学学报（自然科学版）》2007年第5期42-45,共4页Journal of Henan University of Technology：Natural Science Edition

摘　　要：对动物组织来源的苹果酸脱氢酶——猪心肌苹果酸脱氢酶的酶学性质及稳定性进行了研究.结果表明：苹果酸脱氢酶的相对分子质量约为69 000,含有2个亚基,每个亚基的相对分子质量约为34 000;该酶的最适作用pH为8.0,最适作用温度为50℃;Km值为84.6μmol/L（草酰乙酸,pH8.3）.通过对酶的稳定性研究,该酶在50℃以下具有较好的稳定性,其pH稳定范围为7.0-9.0（25℃,20 h）.The enzymatic properties and stability of malate dehydrogenase from porcine heart were investigated. The results showed that molecular weight of malate dehydrogenase was 69 kDa which included two subunits with the molecular weight was about 34 kDa. The optimal pH, temperature and Km were 8.0, 50 ℃ and 84.6μmol/L （oxaloacetic acid, pH 8.3）, respectively. It was indicated that the enzyme was stable with the temperature below 50℃ and the pH range from 7.0 to 9.0（25℃ ,20 h）.

关 键 词：苹果酸脱氢酶 酶学性质 稳定性 猪心 

分 类 号：Q814[生物学—生物工程]