Age changes of isoelectric points of the molecular forms of tyrosine aminotransferase from rat liver.
Hydrocortisone-induced tyrosine aminotransferase was isolated from liver of young and old rats and purified by ammonium sulfate precipitation, heat treatment, DEAE-cellulose chromatography and isoelectric focusing. Isoelectric points of the molecular forms of the enzyme were as follows: pH 4.30, 5.00, 5.72 for young rats and pH 4.25, 4.7, 6.62 and 8.00 for old rats. At 6 days after the initial homogenization only one major peak in tyrosine aminotransferase activity corresponding to an isoelectric point of pH 5.10 can be recognized.
D000375:Aging; D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D007526:Isoelectric Point; D008099:Liver / Q000201:enzymology*; D008297:Male; D011499:Protein Processing, Post-Translational; D051381:Rats; D011919:Rats, Inbred Strains; D014444:Tyrosine Transaminase / Q000032:analysis*
D014444:Tyrosine Transaminase