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Journals / Turkish Journal of Veterinary and Animal Sciences / 2012 / Cilt: 36 - Sayı: 6

Molecular and kinetic characterization of lactate dehydrogenase enzyme in the heart and breast muscle of Japanese quail (Coturnix japonica)

Ram Pratap SINGH
Kochiganti Venkata Hanumat SASTRY
Radha AGARWAL
Nitin Kumar PANDEY
Vishesh Kumar SAXENA
Jag MOHAN
Pages
628–634
Publication Date
2012-06-01
DOI
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AI Summary & Key Takeaways

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⚡ TL;DR(Too Long; Didn't Read)

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.

📌 3 Key Takeaways

🎯
Objective & Hypothesis: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.
📊
Key Findings & Data:Substrate inhibition, enzyme kinetics, and inhibitor (urea) studies indicated that the isozymes present in these tissues differed in their functional properties.
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Conclusion & Impact: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.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Key words: Lactate dehydrogenase · heart · breast muscle

Abstract

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.

Özet

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.

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Cite This Article

SINGH, R. P., SASTRY, K. V. H., AGARWAL, R., PANDEY, N. K., SAXENA, V. K., MOHAN, J. (2012). Molecular and kinetic characterization of lactate dehydrogenase enzyme in the heart and breast muscle of Japanese quail (Coturnix japonica). Turkish Journal of Veterinary and Animal Sciences, Cilt: 36 - Sayı: 6, 628–634. https://ajindex.com/articles/121664

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