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机构地区:[1]北京大学生命科学学院
出 处:《生物化学杂志》1995年第1期85-90,共6页
摘 要:采用8-(6-氨己基)-氨基-5'-AMPSepharose亲和层析法和DEAE-Sepharose离子交换层析法从大熊猫心肌中分离纯化出了乳酸脱氢酶同工酶H4.纯化的大熊猫LDH-H4,比活为445U/mg蛋白,经SDS-PAGE,PAGE,等电聚焦电泳鉴定均为一条带,其亚基分子量为36000,等电点为5.45.经测定大熊猫LDH-H亚基N端被封闭,C端氨基酸残基经测定为Leu.氨基酸组成分析表明每个亚基含有5个Cys,9个Met.Lactate dehydrogenase (LDH EC 1.1.1.27) isozyme H4 was separated and purified from giant panda heart muscle by 8-(6-aminohexyl)-amino-5’-AMPSepharose 4B affinity chromatography and DEAE-Sepharose ion exchange chromatography. 34mg LDH-H4 were obtained from 100g heart muscle. Its specific activity was 445U/mg. The purified LDH-H4 was shown to be homogenous by SDS-PAGE, PAGE and IEF with a pI of 5.45. The subunit has a molecular weight of 36kD. There are 5 Cys and 9 Met in each subunit according to its amino acid compositon analysis.It has a blocked N-terminal and its C-terminal residue is Leu.
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