## Abstract An unusual pattern of LDH isozymes was observed by gel electrophoresis of an extract of a human testis. This isozyme composition is consistent with an allelic variant of Ldh‐c.
Catalytic properties of the sperm-specific lactate dehydrogenase (LDH X or C4) from different species
✍ Scribed by Coronel, Carlos E. ;Burgos, Carlos ;Gerez De Burgos, Nelia M. ;Rovai, Leonor E. ;Blanco, Antonio
- Publisher
- John Wiley and Sons
- Year
- 1983
- Tongue
- English
- Weight
- 502 KB
- Volume
- 225
- Category
- Article
- ISSN
- 0022-104X
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✦ Synopsis
A comparative study of catalytic properties of the sperm-specific lactate dehydrogenase (EC 1.1.1.27) isozyme X or C4 from a variety of animals (boar, bull, goat, Guinea pig, man, mouse, pigeon, rabbit, and rat) is presented. Optimum concentration and Km values for pyruvate, inhibition by substrate, and activity against analog substrates (a-ketoacids with linear and branched chains from 4 to 6 carbon atoms) for isozyme X of different species showed significant differences. The observed properties are correlated with available evidence on the metabolic role of the enzyme.
LITERATURE CITED
Battellino, L.J., and A. Blanco (1970a) Catalytic properties of the lactate dehydrogenase isozyme X from mouse testis.
📜 SIMILAR VOLUMES
## Abstract The sperm‐specific isozyme of murine lactate dehydrogenase (LDH‐C~4~ was injected into female mice of various strains. Two regulatory phenotypes characterize the resultant immunity to LDH‐C~4~: one is manifested by high, intermediate or low levels of response, the other by the immediate