A liver factor that interconverts multiple forms of tyrosine aminotransferase

Three activity peaks of rat liver soluble tyrosine aminotransferase have been resolved using hydroxyl-apatite chromatography. These peaks interconvert during storage of the soluble enzyme preparation in ice for 20 h. A component of a particulate fraction of liver which will interconvert the forms of...

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Veröffentlicht in:Life sciences (1973) 1975-02, Vol.16 (3), p.437-449
Hauptverfasser: Smith, Garry J., Pearce, P.Helen, Oliver, Ivan T.
Format: Artikel
Sprache:eng
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Zusammenfassung:Three activity peaks of rat liver soluble tyrosine aminotransferase have been resolved using hydroxyl-apatite chromatography. These peaks interconvert during storage of the soluble enzyme preparation in ice for 20 h. A component of a particulate fraction of liver which will interconvert the forms of tyrosine aminotransferase in vitro with no alteration of total enzyme activity has been detected. This factor is present in a 31, 000 gh pellet of liver and is solubilized by sonication. When the factor is subjected to dialysis or incubation at 25°C for 30 min. its effect on tyrosine aminotransferase is greatly diminished.
ISSN:0024-3205
1879-0631
DOI:10.1016/0024-3205(75)90265-9