@article{article_5921, title={LENTIL SEED ASPARTATE APvIINOTRANSFERASE ISOENZYMES I. ISOLATION and PARTIAL PURIFICATION}, journal={Journal of Faculty of Pharmacy of Istanbul University}, volume={31}, pages={1–10}, year={2015}, url={https://izlik.org/JA25LZ87ZB}, author={R. Yanardağ**, N. Akev*, A. Can*}, keywords={Lentil, Lens culinaris Medik., aspartate minotransferase, isoenzymes}, abstract={Three electrophoretically distinct aspartate minotransferase isoenzymes
named AAT-1, AAT-2and AAT-3, were separated from lentil (Lens culinaris
Medik.) seeds by extraction, ammonium sulphate precipitation, hydroxylapatite
and DEAE-cellulose column chromatographies. AAT-1 was purified 228,
AAT-2,42 and AAT-3, 3.8 fold. The isoenzymes were examined by means of
polyacrylamide gel electrophoresis.Owing to its key role in general metabolism, aspartate adotransferase (AAT, E.C. 2.6.1.1.) which was formerly called glutamic oxaloacetic transaminase (GOT), occurs widely in nature. In animals, cytbsolic and rnitochon+al forms of AAT have been characterized and purified (1-4). AAT has also been studied in various plants (5, 6) and different isoeozyrnic forms have been r&-, ported. The enzyme has been extensively characterized in wheat germ (7,8), cauliflower (9), cotton seeds (lo), pea (ll), soybean (12-14), oat (15), lupine (16) and alfalfa (17,18).}