Covalent labelling of the protochlorophyllide oxidoreductase from etioplast membranes with (3H)N-phenylmaleimide
[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...
| Main Authors: | , |
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| Format: | Journal Article |
| Published: |
1981
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| Online Access: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1162858/?tool=pubmed http://hdl.handle.net/20.500.11937/21703 |
| _version_ | 1848750664399716352 |
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| author | Oliver, Richard Griffiths, W. |
| author_facet | Oliver, Richard Griffiths, W. |
| author_sort | Oliver, Richard |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | [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. |
| first_indexed | 2025-11-14T07:40:26Z |
| format | Journal Article |
| id | curtin-20.500.11937-21703 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T07:40:26Z |
| publishDate | 1981 |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-217032017-01-30T12:26:49Z Covalent labelling of the protochlorophyllide oxidoreductase from etioplast membranes with (3H)N-phenylmaleimide Oliver, Richard Griffiths, W. [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. 1981 Journal Article http://hdl.handle.net/20.500.11937/21703 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1162858/?tool=pubmed restricted |
| spellingShingle | Oliver, Richard Griffiths, W. Covalent labelling of the protochlorophyllide oxidoreductase from etioplast membranes with (3H)N-phenylmaleimide |
| title | Covalent labelling of the protochlorophyllide oxidoreductase from etioplast membranes with (3H)N-phenylmaleimide |
| title_full | Covalent labelling of the protochlorophyllide oxidoreductase from etioplast membranes with (3H)N-phenylmaleimide |
| title_fullStr | Covalent labelling of the protochlorophyllide oxidoreductase from etioplast membranes with (3H)N-phenylmaleimide |
| title_full_unstemmed | Covalent labelling of the protochlorophyllide oxidoreductase from etioplast membranes with (3H)N-phenylmaleimide |
| title_short | Covalent labelling of the protochlorophyllide oxidoreductase from etioplast membranes with (3H)N-phenylmaleimide |
| title_sort | covalent labelling of the protochlorophyllide oxidoreductase from etioplast membranes with (3h)n-phenylmaleimide |
| url | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1162858/?tool=pubmed http://hdl.handle.net/20.500.11937/21703 |