1 H‐NMR study of the interaction of aminopyrine with purified rat liver microsomal cytochrome P‐450
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 contributi...
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Published in: | FEBS letters Vol. 181; no. 2; pp. 295 - 299 |
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Main Authors: | , , , |
Format: | Journal Article |
Language: | English |
Published: |
25-02-1985
|
Online Access: | Get full text |
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Summary: | 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. |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(85)80279-9 |