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MECHANISTIC STUDIES OF MICROSOMAL NITROSAMINE OXIDATIONS.
Abstract
Since 1954, when Williams [1] first recognized the presence of a carbon monoxide binding pigment in the liver microsomes, much attention has been focused on the structure and function of this ubiquitous protein. Early investigations by Klingenberg [2] and Garfinkel [3] demonstrated that this pigment in the reduced form would combine with carbon monoxide to form a complex absorbing light strongly at 450 nm. Omura and Sato [4,5] established the hemoprotein nature of the pigment, its relatively ready conversion to an inactive form, in which the reduced hemoprotein-carbon monoxide complex absorbed light maximally at 420 nm (cytochrome P-420), and described millimolar extinction coefficients for the two forms.
Subject Area
Biochemistry
Recommended Citation
KROEGER KOEPKE, MARILYN BETH, "MECHANISTIC STUDIES OF MICROSOMAL NITROSAMINE OXIDATIONS." (1978). ETD collection for University of Nebraska-Lincoln. AAI7900329.
https://digitalcommons.unl.edu/dissertations/AAI7900329