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牛蛙乳酸脱氢酶同工酶的分离纯化及其性质研究
引用本文:周静,郑玉才,金素钰.牛蛙乳酸脱氢酶同工酶的分离纯化及其性质研究[J].四川动物,2006,25(2):244-246.
作者姓名:周静  郑玉才  金素钰
作者单位:西南民族大学生命科学与技术学院,成都,610041
摘    要:牛蛙心脏中乳酸脱氢酶在聚丙烯酰胺凝胶电泳上显示3种同工酶区带,分别命名为LDH1、LDH2、LDH3,其中LDH1的活力占绝对优势.采用HiTrap^TM Blue HP 亲和层析和DEAE-Sephadex A离子交换层析对牛蛙骨骼肌中的LDH3进行了分离纯化.纯化的LDH3比活力为295 U/mg,Km NADH=0.028,Km丙酮酸=1.242,在SDS-PAGE上显示两条带,提示该同工酶是由两种亚基组成的,亚基的分子量分别为35.3 kD和37.6 kD.

关 键 词:牛蛙  乳酸脱氢酶  同工酶
文章编号:1000-7083(2006)02-0244-03
收稿时间:2005-10-21
修稿时间:2005年10月21

Purification and Characterizations of Lactate Dehydrogenase Isozyme of Bullfrog
ZHOU Jing,ZHENG Yu-cai,JIN Su-yu.Purification and Characterizations of Lactate Dehydrogenase Isozyme of Bullfrog[J].Sichuan Journal of Zoology,2006,25(2):244-246.
Authors:ZHOU Jing  ZHENG Yu-cai  JIN Su-yu
Institution:College of Life Science and Technology, Southwest University for Nationalities, Chengdu 610041
Abstract:Lactate dehydrogenase of bullfrog heart showed three isozymes on polyacrylamide gel electrophoresis,LDH_1,LDH_2,and LDH_3.LDH_1 exhibited the highest activity.LDH_3 was separated and purified from bullfrog muscle by HiTrap~ TM Blue HP affinity chromatography and DEAE-Sephadex A ion exchange chromatography.The relative activity of purified LDH_3 was 295 U/mg.Protein kinetic analysis showed that the Michaelis constants(Km)value for NADH was 0.028,and Km value for pyruvate was 1.242.The purified LDH_3 exhibited two bands on SDS-PAGE,with molecular weight of 35.3 kD and 37.6 kD respectively,suggesting that the LDH_3 isozyme be composed of two subunits.
Keywords:bullfrog  lactate dehydrogenase  isczyme
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