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NADH CYTOCHROME C REDUCTASE ACTIVITY ASSOCIATED WITH A MEMBRANE FRACTION FROM PROTEIN BODIES OF LUPINUS ANGUSTIFOLIUS COTYLEDONS
Author(s) -
PLANT A. R.,
MOORE K. G.
Publication year - 1983
Publication title -
new phytologist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.742
H-Index - 244
eISSN - 1469-8137
pISSN - 0028-646X
DOI - 10.1111/j.1469-8137.1983.tb03436.x
Subject(s) - biochemistry , cytochrome c , cytochrome , reductase , vesicle , chemistry , biology , membrane , enzyme , mitochondrion
SUMMARY Protein bodies (PBs) were isolated from germinating seeds of Lupinus angustifolius L. (cv. New Zealand Bitter Blue) by centrifugation in an isotonic medium. A membrane vesicle fraction was isolated from the organelle after solubilization of the protein matrix and found to have an associated NADH cytochrome c reductase. The reductase had a broad alkaline pH optimum and NADH was the favoured electron donor ( K m =11.0 μM) whilst ferricyanide, dichlorophenol indophenol and cytochrome c were effective as electron acceptors. Cations were found to enhance (NH 4 + , Li + , Na + , K + , Rb + , Cs + , Mg 2+ ) or decrease (Ca 2+ , Sr 2+ ) the activity. Inhibitor studies enabled the partial characterization of the PB membrane NADH cytochrome c reductase and suggested that it was of a microsomal rather than mitochondrial type.