Literature DB >> 974100

Transaminase of branched chain amino acids. XI. Leucine (methionine) transaminase of rat liver mitochondria.

T Ikeda, Y Konishi, A Ichihara.   

Abstract

An aminotransferase (transaminase) which is active for leucine and methionine, but not for valine or isoleucine, was purified from rat liver mitochondria. The purified preparation appeared homogeneous on polyacrylamide disc gel electrophoresis. Its molecular weight was shown to be 55 000 by gel filtration. It differed from enzyme II (leucine aminotransferase, EC 2.6.1.6) in the supernatant fraction, another transaminase which is also specific for leucine and methionine, in molecular weight, Km values for substrates, electrophoretic mobility, chromatographic behavior and heat stability. From comparison with related transaminases it was concluded to be a new enzyme and named mitochondrial leucine (methionine) transaminase.

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Year:  1976        PMID: 974100     DOI: 10.1016/0005-2744(76)90115-7

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

1.  Methionine transamination--metabolic function and subcellular compartmentation.

Authors:  P W Scislowski; K Pickard
Journal:  Mol Cell Biochem       Date:  1993-12-08       Impact factor: 3.396

2.  Enzymatic and pharmacokinetic studies on the metabolism of branched chain alpha-keto acids in the rat.

Authors:  K H Bässler; A Pietrek
Journal:  Z Ernahrungswiss       Date:  1983-01

3.  Differential alterations in branched-chain amino acid decarboxylation in liver of hypophysectomized rats.

Authors:  S G Sullivan; D A Potter; M R Krauss; J Dancis; R P Cox
Journal:  Experientia       Date:  1979-08-15
  3 in total

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