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Arginase isoforms in frog and lizard tissues.

Gita Venkatakrishnan1, S R R Reddy

  • 1Department of Zoology, University of Pune, Pune 411 007, India. gitavenkatakrishnan@hotmail.com

Indian Journal of Biochemistry & Biophysics
|November 20, 2010
PubMed
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Arginase isoforms in frogs and lizards show functional overlap, challenging the link between nitrogen excretion and specific enzyme sets. Different tissues and species exhibit varied arginase profiles.

Area of Science:

  • Biochemistry
  • Comparative Physiology
  • Enzymology

Background:

  • Arginase, a key enzyme in the urea cycle, exists in multiple isoforms.
  • Understanding arginase isoform distribution and function across species is crucial for metabolic studies.
  • Nitrogen excretion pathways (ureotelism vs. uricotelism) may influence arginase expression.

Purpose of the Study:

  • To investigate and compare arginase isoforms in the liver and kidney of a ureotelic frog (Rana tigerina) and a uricotelic lizard (Calotes versicolor).
  • To analyze the biochemical properties and immunological responses of these arginase isoforms.
  • To evaluate the relationship between nitrogen excretion strategies and arginase isoenzyme profiles.

Main Methods:

  • Fractionation of arginase isoforms using DEAE-cellulose chromatography.

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  • Characterization of isoenzymes by pH optimum, substrate affinity, and molecular weight.
  • Immunoprecipitation assays using antibodies against rat and beef liver arginases.

    • Main Results:

    • Four arginase isoforms (A'1, A2, A3, A4) were identified in lizard liver, while two forms (A2, A3) were found in lizard kidney and both frog tissues.
    • Isoenzymes exhibited similar pH optima, substrate affinities, and molecular weights across species and tissues.
    • Lizard arginase isoforms were poorly recognized by antibodies, whereas frog isoforms showed significant activation.

    Conclusions:

    • The number and types of arginase isoenzymes differ between lizard liver, lizard kidney, and frog tissues.
    • A specific mode of nitrogen excretion (ureotelism or uricotelism) is not directly correlated with a particular set of arginase isoenzymes.
    • The study suggests considerable functional overlap among arginase isoforms, questioning established roles for basic and acidic forms in urea synthesis and other metabolic pathways.