Purification and characterization of microsomal cytochrome b sub(5) and NADH cytochrome b sub(5) reductase from Pisum sativum

Purification and characterization of microsomal cytochrome b sub(5) and NADH cytochrome b sub(5) reductase from Pisum sativum

In this communication the authors document the reproducible protocols for the purification of milligram quantities of cytochrome b sub(5) and NADH-cytochrome b sub(5) reductase from the microsomal fraction of Pisum sativum). The cytochrome B sub(5) component of this NADH linked electron transport ch...

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Veröffentlicht in:Plant physiology (Bethesda) 1987-01, Vol.85 (2), p.457-462
Hauptverfasser: Jollie, DR, Sligar, S G, Schuler, M
Format: Artikel
Sprache:eng
Schlagworte:
cytochrome b5
microsomes
NADH cytochrome b5 reductase
Pisum sativum
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Zusammenfassung:In this communication the authors document the reproducible protocols for the purification of milligram quantities of cytochrome b sub(5) and NADH-cytochrome b sub(5) reductase from the microsomal fraction of Pisum sativum). The cytochrome B sub(5) component of this NADH linked electron transport chain was found to have a molecular mass of 16,400 daltons and the reductase a molecular mass of 34,500 daltons.
ISSN:0032-0889