The flavin-containing monooxygenase expressed in pig liver: primary sequence, distribution, and evidence for a single gene
- 9 January 1990
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 29 (1), 119-124
- https://doi.org/10.1021/bi00453a014
Abstract
The primary sequence of the flavin-containing monooxygenase expressed in pig liver has been derived from the nucleotide sequence of cloned cDNA. The derived sequence is composed of 532 amino acids and represents a protein having a molecular weight of 58,952. The complete sequence was obtained from a single clone containing 2070 bases. A second clone, obtained from an independent library, yielded an identical sequence for the 1374 bases present. The amino acid composition compiled from the derived sequence is very similar to that obtained previously from the purified protein. In addition, a 10 amino acid sequence in a peptide formed from the purified protein by digestion with V8 protease exactly matches the derived sequence for residues 309-318. The flavin-containing monooxygenase expressed in pig liver is also expressed in pig lung and kidney as determined by analysis of both microsomal proteins and mRNA. The ratio of mRNA to protein for the enzyme in kidney is about 5 times greater than the same ratio for liver and about twice the ratio for lung. The reasons for these differences are not understood. Southern analysis of genomic DNA indicates that there is a single gene encoding the flavin-containing monooxygenase expressed in pig liver. Therefore, the broad activity of this enzyme in liver appears to be the result of the catalytic diversity of a single protein.This publication has 20 references indexed in Scilit:
- Catalytic activity and substrate specificity of the flavin-containing monooxygenase in microsomal systems: Characterization of the hepatic, pulmonary and renal enzymes of the mouse, rabbit, and ratArchives of Biochemistry and Biophysics, 1985
- Identification of distinct hepatic and pulmonary forms of microsomal flavin-containing monooxygenase in the mouse and rabbitBiochemical and Biophysical Research Communications, 1985
- Rabbit lung flavin-containing monooxygenase is immunochemically and catalytically distinct from the liver enzymeBiochemical and Biophysical Research Communications, 1984
- Purification of the flavin-containing monooxygenase from mouse and pig liver microsomesInternational Journal of Biochemistry, 1984
- A recovered avian myelocytomatosis virus that induces lymphomas in chickens: pathogenic properties and their molecular basisCell, 1983
- A simple and very efficient method for generating cDNA librariesGene, 1983
- Purification of mixed-function amine oxidase from rat liver microsomesBiochemical and Biophysical Research Communications, 1983
- Glutathione Reductase from Human Erythrocytes. Amino-Acid Sequence of the Structurally Known FAD-Binding DomainEuropean Journal of Biochemistry, 1981
- Isolation of biologically active ribonucleic acid from sources enriched in ribonucleaseBiochemistry, 1979
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979