The sperm-specific lactate dehydrogenase (LDH) isozyme 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.
ASJC Scopus subject areas
- Molecular Biology