@article{30a78f10ae0546469eec1c167133ecd2,
title = "Flavin adenine dinucleotide requirement for kynurenine hydroxylase of rat liver mitochondria",
author = "Hiroshi Okamoto and Osamu Hayaishi",
note = "Funding Information: L-Kynurenine-3-hydroxylase, a monooxygenase, catalyzes the conversion of L-kynurenine to 3-hydroxy-L-kynurenine with the stoichiometric utilization of NADPH and molecular oxygen (De Castro et al., 1956; Saito et al., 1937). Quite recently, data (Okamoto et al., 1967) have been presented to show that kynurenine hydroxylase is localized in the outer membrane fraction of rat liver mitochondria, and that it is possible to achieve about 12-fold concentration of the enzyme activity as compared with that of the original mitochondrial preparation. In this communication, the kynurenine hydroxylase mitochondrial outer membrane fraction was investigated ammonium sulfate treatment. Available evidence indicates 1 This investigation has been from the National in part Cancer by Public Institute, Health Service Research Grants CA-04222, and AM-10333, from the National Institute of Arthritis and Metabolic Diseases; and grants from the Jane Coffin Childs Memorial Fund for Medical Research, the Squibb Institute for Medical Research, and the Scientific Research Fund of the Ministry of Education of Japan.",
year = "1967",
month = nov,
day = "17",
doi = "10.1016/0006-291X(67)90469-X",
language = "English",
volume = "29",
pages = "394--399",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "3",
}