[Coimmobilization of lactate dehydrogenase and low molecular weight thiols on sepharose].
Lactate dehydrogenase (EC 1.1.1.27) and dithiothreitol (DTT) were coimmobilized on Sepharose activated with cyanogen bromide. It was demonstrated that addition of 10 mM DTT (but not 2-mercaptoethanol) during immobilization increased the enzyme specific activity 1.5-5-fold, depending on the initial extent of Sepharose activation by cyanogen bromide. The total activity increased two- to threefold. The lactate dehydrogenase preparations were rich in matrix-immobilized sulfhydryl groups (1.8-13.0 nmol per ml gel). The presence of DTT increased the stability of immobilized lactate dehydrogenase.
Iazykova
M Iu
MIu
Belozerskii Institute of Physico-Chemical Biology, Moscow State University, Moscow, 119899 Russia.
Muronets
V I
VI
D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000302:isolation & purification*; D007770:L-Lactate Dehydrogenase / Q000302:isolation & purification*; D008970:Molecular Weight; D012685:Sepharose; D013438:Sulfhydryl Compounds / Q000302:isolation & purification*
D004800:Enzymes, Immobilized; D013438:Sulfhydryl Compounds; D012685:Sepharose; D007770:L-Lactate Dehydrogenase