@article{oai:omu.repo.nii.ac.jp:00009219,
 author = {FUJII, Michiko and YOSHII, Keiji},
 journal = {Bulletin of the University of Osaka Prefecture. Ser. B, Agriculture and life sciences},
 month = {Mar},
 note = {application/pdf, Alanine aminotransferase from germinating castor bean endosperms was purified about 1,500-fold by ammonium sulfate fractionation and chromatographies with DEAE-Sepharose CL-6B, TEAE-Cellulose, QAE-Sephadex A-50, and TSK-5PW (HPLC). The molecular weight of the enzyme was about 110kDa, with two identical subunits. The purified enzyme was highly specific for alanine as an amino donor and 2-oxoglutarate as an acceptor, and it showed also glyoxylate transamination activities at low rate. The evidence indicates that alanine: 2-oxoglutarate aminotransferase and glyoxylate aminotransferase activities are associated with the same protein. Pyridoxal phosphate as a cofactor was so tightly bound to the enzyme that added pyridoxal phosphate was not required in the assays. The enzyme showed normal Michaelis-Menten kinetics for all substrates. Reactions proceeded by a Ping Pong Bi Bi mechanism. The K_m for L-alanine, 2-oxoglutarate were 3.4mM and 0.26mM, respectively. The optimum pH was 8.5 and pI was about 4.6., Bulletin of the University of Osaka Prefecture. Ser. B, Agriculture and life sciences. 1995, 47, p.95-104},
 pages = {95--104},
 title = {Purification and Properties of Alanine aminotransferase from Germinating Castor Bean Endosperms},
 volume = {47},
 year = {1995}
}