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Rat mammary arginase: isolation and characterization

C P Jenkinson1, M R Grigor

  • 1Department of Biochemistry, University of Otago, Dunedin, New Zealand.

Biochemical Medicine and Metabolic Biology
|April 1, 1994
PubMed
Summary

Researchers isolated extrahepatic arginase (AII) from rat mammary glands, finding it distinct from hepatic arginase (AI). Mammary AII activity significantly increased during lactation, suggesting de novo synthesis.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Arginase enzymes play crucial roles in urea cycle and nitric oxide synthesis.
  • Extrahepatic arginase isoforms have been identified, but their specific functions and regulation remain under investigation.
  • Mammary gland arginase activity exhibits significant changes during lactation.

Purpose of the Study:

  • To isolate and characterize the extrahepatic arginase (AII) from rat mammary gland.
  • To compare the properties of mammary arginase (AII) with hepatic arginase (AI).
  • To investigate the regulation of mammary arginase activity during lactation.

Main Methods:

  • Isolation and purification of mammary arginase (AII).
  • Ion exchange chromatography for isozyme separation.
  • Kinetic analysis (pH optima, Km).
  • Isoelectric focusing (pI) and SDS-PAGE for subunit size determination.
  • Solution immunoprecipitation and Western immunoblotting for protein quantification.

Main Results:

  • Mammary arginase activity increased 300% at mid-lactation, independent of liver arginase activity.
  • Two mammary arginase isozymes were identified; the major form, AII, was purified.
  • Arginase AII exhibited kinetic similarity to AI but differed in isoelectric point and subunit size.
  • Mammary and kidney tissues contained both AI and AII, while liver primarily contained AI.
  • Increased mammary arginase AII protein levels correlated with increased activity, suggesting de novo synthesis or reduced degradation.

Conclusions:

  • Mammary gland expresses a distinct extrahepatic arginase (AII) that is upregulated during lactation.
  • The increased activity is likely due to de novo synthesis of arginase AII protein.
  • These findings contribute to understanding tissue-specific arginase regulation and function.

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