Turkish Journal of Veterinary & Animal Sciences




In the present investigation, attempts were made to characterize lactate dehydrogenase (LDH) isozyme in quail heart and breast muscle by using electrophoresis, kinetic, and molecular techniques. Polyacrylamide gel electrophoresis of the heart and breast muscle revealed a single isozyme. Kinetic studies were carried out for further functional characterization of LDH isozyme in the heart and breast muscle. Substrate inhibition, enzyme kinetics, and inhibitor (urea) studies indicated that the isozymes present in these tissues differed in their functional properties. LDH isozyme present in the heart and breast muscle exhibited properties of LDH-A and LDH-B isozyme, respectively. Furthermore, RT-PCR amplification of Ldh-a and Ldh-b mRNA in both tissues confirmed that these isozymes were formed by the association of both H and M subunits and may be of H3M1 and M3H1 in the heart and breast muscle, respectively.


Lactate dehydrogenase, heart, breast muscle, enzyme kinetics, polymerase chain reaction

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