@article{oai:ir.kagoshima-u.ac.jp:00007831,
 author = {SAMESHIMA, Muneo and NAKASHIMA, Hiroyasu},
 journal = {鹿児島大学水産学部紀要=Memoirs of Faculty of Fisheries Kagoshima University},
 month = {2016-10-28},
 note = {Partial purification of GOT isozymes from T. zillii were performed by mean of
CM-cellulose column chromatography. Purified s-GOT and m-GOT fractions showed
remains of a small amount of impurities on disc electrophoregrams. Zymograms of s-GOT
and m-GOT fractions on starch-gel showed their specific polarities. s-GOT fraction yielded
four bands on the anode side of the zymogram, whereas the m-GOT fraction yielded two
bands on the cathode side. Purification of GOT of eel liver which was performed in order
to compare with the GOT isozymes of tilapia liver. The GOT isozymes of eel liver had
almost same characteristics as that of the tilapia liver.
Kinetic studies on s-GOT and m-GOT from liver of T. zillii were performed. It was
recognized that the reaction of GOT isozyme is a binary mechanism, namely, s-GOT had a
strong affinity for 2-oxoglutarate, whereas m-GOT had a strong affinity for aspartate.},
 pages = {97--107},
 title = {Purification of Aspartate Aminotransferase in the Liver of Tilapia zillii},
 volume = {32},
 year = {}
}