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Animal Reproduction and Physiology
Asian-Australasian Journal of Animal Sciences 2011;24(8): 1060-1068.
DOI: https://doi.org/10.5713/ajas.2011.10263    Published online June 22, 2011.
Molecular Characterization and Expression of LDHA and LDHB mRNA in Testes of Japanese Quail (Coturnix japonica)
R. P. Singh, K. V. H. Sastry, N. K. Pandey, N. G. Shit, R. Agarwal, R. Singh, S. K. Sharma, V. K. Saxena, Jagmohan
Abstract
The LDH isozymes are key catalysts in the glycolytic pathway of energy metabolism. It is well known that the distribution of the LDH isozymes vary in accordance with the metabolic requirements of different tissues. The substrates required for energy production change noticeably at successive stages of testes development suggesting a significant flexibility in the expression of glycolytic enzymes. Therefore, expression of LHDA and LDHB mRNAs was examined in adult and prepubertal quail testis. The mRNA of both LDHA and LDHB were expressed and no significant difference was observed in prepubertal testes. The mRNA levels of LDHB significantly increased during testicular development. In the adult testis, LDHA mRNA was not expressed. Expression studies revealed the presence of different LDH isozymes during testicular development. In contrast, electrophoresis of both testicular samples revealed only single band at a position indicative of an extreme type of LDH isozyme in quail testes. Furthermore, nucleotide and amino acid sequence analysis revealed significant similarity to chicken, duck and rock pigeon. These sequence results confirmed the similarity of LDHA and LDHB subunit protein in different avian species.
Keywords: Lactate Dehydrogenase; Testes; Lactate; Isozymes; Messenger RNA


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