Expression, purification, and characteristics of mammalian protoporphyrinogen oxidase.
Dailey
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TA
Department of Biochemistry and Molecular Biology, University of Georgia, Athens 30602-7229, USA.
Dailey
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HA
D000595:Amino Acid Sequence; D000818:Animals; D004579:Electron Transport; D004926:Escherichia coli / Q000235:genetics; D005420:Flavoproteins; D006801:Humans; D007700:Kinetics; D051379:Mice; D024101:Mitochondrial Proteins; D008969:Molecular Sequence Data; D015394:Molecular Structure; D016296:Mutagenesis; D010088:Oxidoreductases / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism*; D044925:Oxidoreductases Acting on CH-CH Group Donors; D017094:Porphyrias, Hepatic / Q000235:genetics; D050768:Protoporphyrinogen Oxidase; D011524:Protoporphyrins / Q000138:chemical synthesis / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013053:Spectrophotometry
D005420:Flavoproteins; D024101:Mitochondrial Proteins; D011524:Protoporphyrins; D011994:Recombinant Proteins; C011539:protoporphyrinogen; C028025:protoporphyrin IX; D010088:Oxidoreductases; D044925:Oxidoreductases Acting on CH-CH Group Donors; C493978:PPOX protein, human; C493979:Ppox protein, mouse; D050768:Protoporphyrinogen Oxidase