Substrate binding to solubilized cytochrome P-450 from rabbits at different temperatures.
The binding affinities of selected type I- and type II-substrates to partially purified cytochrome p-450 from rabbit liver microsomes were studied and found to differ from those of rats. The temperature dependence of the apparent binding constants qualitatively exhibited the same characteristics compared with that of rats. For type I-substrates endothermic and for type II-substrates exothermic reaction characteristics were observed. Taking into account the partition coefficients of the substrates so far investigated it is obvious that type I substrates with increasing hydrophobicity are bound more strongly while type II-substrates show a more complicated behvaiour. This may due to the fact that other types of binding are included besides the hydrophobic interactions.
D000818:Animals; D001665:Binding Sites; D002021:Buffers; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008862:Microsomes, Liver / Q000201:enzymology; D008970:Molecular Weight; D011817:Rabbits; D051381:Rats; D013696:Temperature
D002021:Buffers; D003577:Cytochrome P-450 Enzyme System