Characteristics of hepatic serine pyruvate aminotransferase in different mammalian species

T. Noguchi, Y. Takada, R. Kido

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

Serine pyruvate aminotransferase was purified from mouse, rat, dog and cat liver. Each enzyme preparation was homogeneous as judged by polyacrylamide disc gel electrophoresis in the presence of sodium dodecyl sulphate. However, isoelectric focusing resulted in the detection of two or more active forms from enzyme preparations from dog, cat and mouse. A single active form was obtained with the rat enzyme. All four enzyme preparations had similar pH optima and molecular weights. Both mouse and rat preparations catalysed transamination between a number of L amino acids (serine, leucine, asparagine, methionine, glutamine, ornithine, histidine, phenylalanine or tyrosine) and pyruvate. Effective amino acceptors were pyruvate, phenylpyruvate and glyoxylate with serine as amino donor. The reverse transamination activity, with hydroxypyruvate and alanine as substrates, was lower than with serine and pyruvate for both species. Serine pyruvate aminotransferase activities were inhibited by isonicotinic acid hydrazide. In contrast, both dog and cat enzyme preparations were highly specific for serine as amino donor with pyruvate, and utilized pyruvate and glyoxylate as effective amino acceptors. A little activity was detected with phenylpyruvate. The reverse activity was higher than with serine and pyruvate for both species. Serine pyruvate aminotransferase activities were not inhibited by isonicotinic acid hydrazide.

Original languageEnglish
Pages (from-to)609-614
Number of pages6
JournalBiochemical Journal
Volume161
Issue number3
Publication statusPublished - 1977
Externally publishedYes

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serine-pyruvate aminotransferase
Pyruvic Acid
Serine
Liver
Enzymes
Rats
Cats
Isoniazid
Dogs
Disc Electrophoresis
Ornithine
Asparagine
Isoelectric Focusing
Electrophoresis
Glutamine
Phenylalanine
Histidine
Leucine
Sodium Dodecyl Sulfate
Alanine

ASJC Scopus subject areas

  • Biochemistry

Cite this

Characteristics of hepatic serine pyruvate aminotransferase in different mammalian species. / Noguchi, T.; Takada, Y.; Kido, R.

In: Biochemical Journal, Vol. 161, No. 3, 1977, p. 609-614.

Research output: Contribution to journalArticle

Noguchi, T, Takada, Y & Kido, R 1977, 'Characteristics of hepatic serine pyruvate aminotransferase in different mammalian species', Biochemical Journal, vol. 161, no. 3, pp. 609-614.
Noguchi, T. ; Takada, Y. ; Kido, R. / Characteristics of hepatic serine pyruvate aminotransferase in different mammalian species. In: Biochemical Journal. 1977 ; Vol. 161, No. 3. pp. 609-614.
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