Abstract:
:In this communication we document the reproducible protocols for the purification of milligram quantities of cytochrome b(5) and NADH-cytochrome b(5) reductase from the microsomal fraction of Pisum sativum. The cytochrome b(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. These components could be reconstituted into a functional NADH oxidase activity active in the reduction of exogenous cytochrome c or ferricyanide. In the latter assay the purified reductase exhibited a turnover number of 22,000 per minute. The amino-terminal amino acid sequence of the cytochrome b(5) component was determined by sequential Edmund degredation, thus providing crucial information for the efficient cloning of this central protein of plant microsomal electron transfer.
journal_name
Plant Physioljournal_title
Plant physiologyauthors
Jollie DR,Sligar SG,Schuler Mdoi
10.1104/pp.85.2.457subject
Has Abstractpub_date
1987-10-01 00:00:00pages
457-62issue
2eissn
0032-0889issn
1532-2548journal_volume
85pub_type
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