Characteristics of purified protoporphyrinogen oxidase from barley

The membrane bound enzyme oxidizing protoporphyrinogen to protoporphyrin, a step in heme and chlorophyll synthesis, was purified to a single prominent polypeptide band on SDS/PAGE from barley mitochondrial fractions. It contained a variety of lipids including 0.66 mg of phosphatidyl ethanolamine and...

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Veröffentlicht in:	Biochemical and biophysical research communications 1989-06, Vol.161 (2), p.790-796
Hauptverfasser:	Jacobs, Nicholas J., Borotz, Susan E., Jacobs, Judith M.
Format:	Artikel
Sprache:	eng
Schlagworte:	ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Analytical, structural and metabolic biochemistry Biological and medical sciences Chelating Agents - pharmacology Cytochromes - analysis Edible Grain - enzymology Enzymes and enzyme inhibitors ENZYMIC ACTIVITY Flavins - analysis Fundamental and applied biological sciences. Psychology Glutathione - pharmacology Hordeum - enzymology HORDEUM VULGARE Iron - analysis Mitochondria - analysis NADH NADPH NUCLEOTIDE NUCLEOTIDES NUCLEOTIDOS Oxidation-Reduction OXIDOREDUCTASES Oxidoreductases - isolation & purification Oxidoreductases Acting on CH-CH Group Donors OXIDORREDUCTASAS OXYDOREDUCTASE Phospholipids - analysis Protoporphyrinogen Oxidase
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