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
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Sprache:eng
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cytochrome b5
microsomes
NADH cytochrome b5 reductase
Pisum sativum
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container_title Plant physiology (Bethesda)
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creator Jollie, DR
Sligar, S G
Schuler, M
description 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.
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source Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Jstor Complete Legacy; Alma/SFX Local Collection
subjects cytochrome b5
microsomes
NADH cytochrome b5 reductase
Pisum sativum
title Purification and characterization of microsomal cytochrome b sub(5) and NADH cytochrome b sub(5) reductase from Pisum sativum
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