Partial Purification and Properties of Alanine and Aspartate Aminotransferases in the Midgut Tissue of the Silkworm, Bombyx mori (Lepidoptera : Bombycidae)

概要

論文の詳細を見る
Alanine aminotransferase (E.C. 2.6.1.2.) and aspartate aminotransferase (E.C. 2.6.1.1.) extracted from the midgut of the silkworm were partially purified approximately 120-fold. The molecular weights of alanine AT-ase and aspartate AT-ase were 69,000 and 68,000,and the optimum pH values were 7.6 and 7.0,respectively. The K_m values of alanine At-ase for alanine and α-ketoglutarate were 6.2×10^<-3>M and 2.3×10^<-4>M, and the K_m values of aspartate AT-ase for aspartate and α-ketoglutarate were 3.6×10^<-4>M and 2.0×10^<-4>M. Hydroxylamine inhibited alanine AT-ase activity and enzyme activity was recovered by pyridoxal-P. Alanine AT-ase inhibited by p-CMB was reactivated by the addtion of DTT.
日本応用動物昆虫学会の論文
1986-05-25