Identification and amino acid sequences of tryptic peptides of a novel ferredoxin-NADP+ oxidoreductase from rice.
A 37-kDa protein purified from rice thylakoid membranes has been identified as a ferredoxin-NADP+ oxidoreductase based on its catalysis of the reduction of nitro blue tetrazolium via NADPH and its recognition by antibodies against ferredoxin-NADP+ oxidoreductase. Amino acid sequences determined from tryptic fragments of the enzyme further confirm the identity of the protein and show the presence of unique sequences at the amino-terminus.
Swegle
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Plant Molecular Biology Laboratory, United States Department of Agriculture/Agriculture Research Service-REE, Beltsville Agricultural Research Center (W), MD 20705-2350, USA.
Mattoo
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AK
D000595:Amino Acid Sequence; D001483:Base Sequence; D005287:Ferredoxin-NADP Reductase / Q000737:chemistry* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D012275:Oryza / Q000201:enzymology*; D010455:Peptides / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D017386:Sequence Homology, Amino Acid; D014357:Trypsin / Q000378:metabolism*
D010455:Peptides; D010940:Plant Proteins; D005287:Ferredoxin-NADP Reductase; D014357:Trypsin