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Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure. 536:226-234
The LM-2 fraction of cytochrome P-450 from rabbits in the presence and in the absence of substrate (benzphetamine) is shown to be a thermal mixture of a high spin ( S = 5 2 ) and a low spin ( S = 1 2 ) form each of which exhibiting its individual opt
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 708:42-48
The binding of an active-site-targeted spin-labeled compound to cytochrome P -450 showing type I spectral characteristics in its optical difference spectrum was studied by optical and EPR spectroscopy and compared with that of other spin-labeled subs
Publikováno v:
Xenobiotica. 19:1231-1246
1. The anaerobic NADPH-reduction of the isozymes cytochrome P-450 LM2 and LM4 was used as a functional tool to study the component interaction in reconstituted monooxygenase systems in dependence on different phospholipids. 2. The isozymes were shown
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure. 236:211-221
The influence of several anions, such as ATP, 2,3-diphosphoglycerate, inositol hexaphosphate, K4[Fe(CN)6] and K3[Co(CN)6], on the O2 binding of Hb A and the binding of n-propyl isocyanide to Hb A dependent upon pH was investigated. Known organic anio
Publikováno v:
FEBS Letters. (2):173-176
Publikováno v:
FEBS Letters. (2):309-312
In the mixed function oxidase reaction molecular oxygen is activated by an as yet unknown mechanism [l] . The stoichiometry suggests that activated oxygen exists at the redox level of peroxide or atomic oxygen (oxene). Although hydrogen peroxide was
Publikováno v:
FEBS letters. 83(1)
Publikováno v:
Acta biologica et medica Germanica. 37(4)
Species dependencies and the temperature function of substrate binding reaction have been studied. The solubilized P-450 preparations from rat and rabbit, respectively, exhibit similar substrate binding characteristics with respect to rate constants
Publikováno v:
Biomedica biochimica acta. 43(12)
Fluorescein isothiocyanate was selectively bound to the epsilon-amino group of a lysine residue of cytochrome P-450 LM2 at rho H 8.15. The decrease in the N-demethylase activity after modification evidences the functional importance of the modified g