VOPROSY MEDITSINSKOI KHIMII (ISSN 0042-8809)

Kinetic properties of lipoamide dehydrogenase of the oxoglutarate dehydrogenase complex of the human heart

   
Ostrovtsova S.A., Strumilo S.A.
PubMed Id: 1858346
Year: 1991  Volume: 37  Issue: 1  Pages: 70-71
Kinetics of lipoamide dehydrogenase catalyzed reaction is described by Michaelis-Menten equation if concentrations of NAD and dihydrolipoamide (DLA) varied. Effective Km values were equal to 0.11 mM for NAD and 0.50 mM for DLA, respectively. Kinetic indications of positive cooperation between sites binding both NAD and DLA were manifested in presence of NADH. Apparent Ki value for NADH constituted 0.88-0.10 mM, thus demonstrating the effective regulation of the lipoamide dehydrogenase activity by end products.
Download PDF:  
Citation:

Ostrovtsova, S. A., Strumilo, S. A. (1991). Kinetic properties of lipoamide dehydrogenase of the oxoglutarate dehydrogenase complex of the human heart. Voprosy Meditsinskoi Khimii, 37(1), 70-71.
References
 2002 (vol 48)
 2001 (vol 47)
 2000 (vol 46)
 1999 (vol 45)
 1998 (vol 44)
 1997 (vol 43)
 1996 (vol 42)
 1995 (vol 41)
 1994 (vol 40)
 1993 (vol 39)
 1992 (vol 38)
 1991 (vol 37)
 1990 (vol 36)
 1989 (vol 35)
 1988 (vol 34)
 1987 (vol 33)
 1986 (vol 32)
 1985 (vol 31)
◄        ►