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Mitochondrial membrane-bound activity of arginase is independent of nitrogen excretion pattern in ureogenic and non-ureogenic vertebrates.

Authors
  • Suman, Mishra
  • Rajnikant, Mishra
Type
Published Article
Journal
Indian journal of experimental biology
Publication Date
Feb 01, 2017
Volume
55
Issue
2
Pages
74–78
Identifiers
PMID: 30183231
Source
Medline
Language
English
License
Unknown

Abstract

Arginase, that regulates metabolism of arginine, is widely distributed in organisms. The two major isoforms, cytosolic Arginase-I, and mitochondrial Arginase-II have been characterized well. However, reports also suggest another mitochondrial membrane-bound arginase which is extracted by washing the mitochondria with KCl. Here, we studied this mitochondrial membrane-bound arginase among vertebrates. Our observations support that arginase activity is predominant in cytosol which is designated as Arginase-I. The mitochondrial membrane-bound Arginase (mbArg) which resembles Arginase-II seems independent of nitrogen excretion pattern because of its presence both in ureogenic and non-ureogenic vertebrates.

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