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Lactate dehydrogenase isozyme patterns in the denervated quail (Coturnix coturnix japonica) muscles

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Abstract

Polyacrylamide gel electrophoresis of the Japanese quail (Coturnix cotunix japonica) muscle extracts revealed a single lactate dehydrogenase isozyme. A month after surgical unilateral brachiotectomy (denervation) there was significant atrophy of the triceps, biceps and radius ulnar muscles accompanied by the appearance of an additional lactate dehydrogenase isozyme band. This extra band may be the result of the synthesis of a new lactate dehydrogenase isozyme. This new isozyme exhibited a lower affinity for lactate, less sensitivity to urea denaturation and was more thermostable than the lactate dehydrogenase of normal (innervated) quail muscles. Based on these properties, it is suggested that the newly synthesised isozyme of the denervated muscles is LDH-1, (or B4/H4) type. Brachiotectomy also resulted in significant quantitative changes in the total lactate dehydrogenase activity of innervated muscles of the same animal.

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Abbreviations

LDH:

Lactate dehydrogenase

BSA:

bovine serum albumin

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Authors and Affiliations

  1. Department of Biochemistry, University of Agricultural Sciences, 560065, G.K.V.K., Bangalore, India

    Abdul Quaium, T. K. Virupaksha, R. V. Krishnamoorthy & L. Sudharshana

  2. Department of Zoology, University of Agricultural Sciences, 560065, G.K.V.K., Bangalore, India

    R. V. Krishnamoorthy

Authors
  1. Abdul Quaium
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  2. T. K. Virupaksha
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  3. R. V. Krishnamoorthy
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  4. L. Sudharshana
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Quaium, A., Virupaksha, T.K., Krishnamoorthy, R.V. et al. Lactate dehydrogenase isozyme patterns in the denervated quail (Coturnix coturnix japonica) muscles. J Biosci 15, 323–328 (1990). https://doi.org/10.1007/BF02702674

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  • DOI: https://doi.org/10.1007/BF02702674

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