LACTATE DEHYDROGENASES IN SPERMATOZOA - SUBUNIT INTERACTIONS IN VITRO
LACTATE DEHYDROGENASES IN SPERMATOZOA - SUBUNIT INTERACTIONS IN VITRO
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DOI：
10.1016/0003-9861(65)90298-5
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发表时间：
1965-01-01
影响因子：
3.9
通讯作者：
GOLDBERG, E
中科院分区：
文献类型：
--
作者：
GOLDBERG, E
精子特异性乳酸脱氢酶（LDH）同工酶从人、牛和鼠的来源已解离，其亚基已重组与亚基从其他形式的酶。生成新的LDH，并根据底物和辅酶的特异性进行了表征。这些新分子的性质反映了它们的亚基组成，而亚基组成又直接或间接地决定了酶的催化位点的特征。本文报道的观察结果表明，精子特异性LDH含有与LDH 1、2、3、4和5不同的多肽亚基。
The sperm-specific lactate dehydrogenase (LDH) iso-zyme from human bovine, and murine sources has been dissociated, and its subunits have been recombined with subunits from the other forms of the enzyme. New LDH''s are generated and have been characterized on the basis of substrate and coenzyme specificity. The properties of these new molecules are a reflection of their subunit composition, which, in turn, must determine either directly or indirectly the characteristics of the catalytic site (s) of the enzyme. The observations reported here demonstrate that the sperm-specific LDH contains polypeptide subunits which differ from those in LDH 1,2,3,4, and 5.