Cloning and nucleotide sequence of a cDNA of the human erythrocyte NADPH-flavin reductase.
A cDNA of human erythrocyte NADPH-flavin reductase was cloned from a lambda gt 11 human reticulocyte cDNA library by polymerase chain reaction using degenerate primers and followed by a plaque hybridization. The nucleotide sequence of the cDNA contains an open reading frame of 621 base pairs which encodes 206 amino acid residues including an initial methionine. The amino acid sequence deduced from the base sequence coincided well with peptide sequence determined for the purified human erythrocyte NADPH-flavin reductase. A homologous sequence to the FMN-binding site of flavodoxins was found at the amino-terminal region.
Chikuba
K
K
Department of Biochemistry, Oita Medical University, Japan.
Yubisui
T
T
Shirabe
K
K
Takeshita
M
M
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular / Q000379:methods; D017931:DNA Primers; D018076:DNA, Complementary / Q000032:analysis; D004912:Erythrocytes / Q000201:enzymology*; D038181:FMN Reductase; D015723:Gene Library; D006801:Humans; D008969:Molecular Sequence Data; D009247:NADH, NADPH Oxidoreductases / Q000096:biosynthesis / Q000097:blood* / Q000737:chemistry; D009928:Organ Specificity; D016133:Polymerase Chain Reaction; D051381:Rats; D012156:Reticulocytes / Q000201:enzymology*; D017386:Sequence Homology, Amino Acid
D017931:DNA Primers; D018076:DNA, Complementary; D038181:FMN Reductase; D009247:NADH, NADPH Oxidoreductases