1H-NMR study of the interaction of aminopyrine with purified rat liver microsomal cytochrome P-450.
Longitudinal relaxation (T1) measurements for all lines (N(CH3)2, N(CH3), C(CH3), phenyl) in the aminopyrine 1H-NMR spectrum were used to study the interaction of aminopyrine with purified microsomal cytochrome P-450 from livers of phenobarbital-treated rats. The paramagnetic contribution to the observed T1(-1) values was determined from its dependence on aminopyrine concentration. The Solomon-Bloembergen equation was used to calculate between Fe3+ and aminopyrine distances in the enzyme-substrate complex. For all protons these distances are about 8 A.
D000632:Aminopyrine / Q000378:metabolism*; D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology*; D051381:Rats; D011919:Rats, Inbred Strains
D000632:Aminopyrine; D003577:Cytochrome P-450 Enzyme System