• Publications
  • Influence
Lipoxygenase - a versatile biocatalyst for biotransformation of endobiotics and xenobiotics
  • A. Kulkarni
  • Chemistry, Medicine
  • Cellular and Molecular Life Sciences CMLS
  • 1 November 2001
Available data suggest that lipoxygenases contribute to in vivo metabolism of xenobiotics in mammals, and a direct hydrogen abstraction by the enzyme and the peroxyl radical-dependent chemical oxidation appear to be central to the co-oxidase activity of lipoxyGENases. Expand
Metabolism of insecticides by mixed function oxidase systems.
Cytochrome P-450 difference spectra: effect of chemical structure on type II spectra in mouse hepatic microsomes.
A comprehensive study of the relationship between chemical structure and binding was made with mouse hepatic microsomes, showing that as substituents are placed closer to this nitrogen, spectral size is either reduced or eliminated. Expand
Predicting rodent carcinogenicity of halogenated hydrocarbons by in vivo biochemical parameters.
Evidence shows that nongenotoxic carcinogenesis is best predicted by nonganotoxic parameters such as CP or CT (components of the predictor TS). Expand
Metabolic fate of chemical mixtures. I. "Shuttle Oxidant" effect of lipoxygenase-generated radical of chlorpromazine and related phenothiazines on the oxidation of benzidine and other xenobiotics.
  • J. Hu, A. Kulkarni
  • Chemistry, Medicine
  • Teratogenesis, carcinogenesis, and mutagenesis
  • 2000
Preliminary data suggest that purified human term placental lipoxygenase also displays a similar stimulatory response in the benzidine oxidation in the presence of chlorpromazine, and whether such a synergistic interaction occurs in humans in vivo is worth pondering. Expand
Cytochrome P-450 difference spectra. Type II interactions in insecticide-resistant and -susceptible houseflies.
The relationship between chemical structure and the difference spectra obtained with microsomes from the abdomens of insecticide-susceptible and -resistant houseflies was examined. The presence of aExpand
Occurrence and characterization of microsomal cytochrome P-450 in several vertebrate and insect species.
Both quantitative and qualitative differences exist between the microsomal cytochrome P-450s of various animal species but differences in enzyme activity cannot be correlated with any single spectral characteristic. Expand
Spectral characterization of microsomal cytochrome P-450 from the midgut of the tobacco hornworm, Manduca sexta J.
The study of type II optical difference spectra using several ligands revealed that the basic requirements for this perturbation are the same as in other animal species, namely, a sterically accessible sp2 or sp3 nitrogen atom. Expand