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dc.contributor.authorOliver, Richard
dc.contributor.authorGriffiths, W.
dc.date.accessioned2017-01-30T12:26:49Z
dc.date.available2017-01-30T12:26:49Z
dc.date.created2010-11-12T02:04:10Z
dc.date.issued1981
dc.identifier.citationOLIVER RP & GRIFFITHS WT (1981) Covalent labelling of the protochlorophyllide oxidoreductase from etioplast membranes with (3H)N-phenylmaleimide. Biochemical Journal 195 93-101
dc.identifier.urihttp://hdl.handle.net/20.500.11937/21703
dc.description.abstract

[3H]N-Phenylmaleimide has been used to covalently label in a specific manner the substrate-protected thiol groups of the enzyme protochlorophyllide reductase. In membrane preparations from oat (Avena sativa) and runner-bean (Phaseolus vulgaris) seedlings, two related peptides of mol.wts. 35000/37000 and 34000/35000 respectively and showing properties expected of the reductase have been identified, whereas the same technique with barley (Hordeum vulgare) extracts resulted in labelling a single peptide of mol.wt. 38000. Evidence is presented that both NADPH and protochlorophyllide are required for protection of the essential thiol groups on the reductase in oat extracts, a situation favouring a ternary complex as the structure for the photoactive enzyme--substrates intermediate.

dc.relation.urihttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC1162858/?tool=pubmed
dc.titleCovalent labelling of the protochlorophyllide oxidoreductase from etioplast membranes with (3H)N-phenylmaleimide
dc.typeJournal Article
curtin.note

A copy of this item may be available from Professor Richard Oliver

curtin.note

Email: Richard.oliver@curtin.edu.au

curtin.accessStatusFulltext not available
curtin.facultyDepartment of Environmental & Agriculture
curtin.facultySchool of Agriculture and Environment
curtin.facultyFaculty of Science and Engineering


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