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1 H‐NMR study of the interaction of aminopyrine with purified rat liver microsomal cytochrome P‐450
Author(s) -
Woldman Ya.Yu.,
Weiner L.M.,
Gulyaeva L.F.,
Lyakhovich V.V.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80279-9
Subject(s) - chemistry , microsome , cytochrome , phenobarbital , substrate (aquarium) , relaxation (psychology) , enzyme , biochemistry , medicine , oceanography , geology , psychology , social psychology , pharmacology
Longitudinal relaxation ( T 1 ) measurements for all lines (N(CH 3 ) 2 , N(CH 3 ), (C(CH 3 ), phenyl) in the aminopyrine 1 H‐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 t 1 −1 values was determined from its dependence on aminopyrine concentration. The Solomon‐Bloembergen equation was used to calculate between Fe 3+ and aminopyrine distances in the enzyme‐substrate complex. For all protons these distances are about 8 Å.