The evolution of peroxisomal and mitochondrial alanine

Glyoxylate aminotransferase 1 in mammalian liver

Yoshikazu Takada, Tomoo Noguchi

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Immunological distances of alanine: glyoxylate aminotransferase 1 (serine:pyruvate aminotransferase) in mitochondria or peroxisomes from eight different mammalian liver were determined with rabbit anti-serum against the mitochondrial enzyme of rat liver by microcomplement fixation. Results suggest that heterotopic alanine:glyoxylate aminotransferase 1 are orthologous proteins and their subcellular localization and substrate specificity changed during rapid molecular evolution.

Original languageEnglish
Pages (from-to)153-157
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume108
Issue number1
DOIs
Publication statusPublished - Sep 16 1982
Externally publishedYes

Fingerprint

serine-pyruvate aminotransferase
Liver
Mitochondria
Peroxisomes
Molecular Evolution
Substrate Specificity
Rats
Rabbits
Substrates
Enzymes
Serum
Proteins
Alanine-glyoxylate transaminase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

The evolution of peroxisomal and mitochondrial alanine : Glyoxylate aminotransferase 1 in mammalian liver. / Takada, Yoshikazu; Noguchi, Tomoo.

In: Biochemical and Biophysical Research Communications, Vol. 108, No. 1, 16.09.1982, p. 153-157.

Research output: Contribution to journalArticle

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