| The proteolytic degradation in vitro of the NADPH-protochlorophyllide oxidoreductase of barley (Hordeum vulgare L.). | |
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MedLine Citation:
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PMID: 6696447 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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A cell-free membrane system has been developed from isolated barley etioplasts which displays a highly selective decrease of the NADPH-protochlorophyllide oxidoreductase in vitro which is indistinguishable from that observed previously in the intact plant. The rapid breakdown of the enzyme protein in vitro is caused by a membrane-bound proteolytic activity. The protease is essentially independent of pH in the physiological pH range of 6 to 8.5. The optimum temperature for the reaction is approximately 40 degrees C. In the presence of excessive protochlorophyllide the enzyme is no longer degraded or inactivated during illumination of dark-grown plants. In the isolated membrane fraction protochlorophyllide also enhances the stability of the enzyme, a similar effect is exerted by NADPH but not by NADH. The results suggest that the inactivation of the NADPH-protochlorophyllide oxidoreductase is influenced by the interaction of the enzyme with protochlorophyllide and NADPH. In the absence of these two components the enzyme becomes susceptible to proteolytic degradation. |
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Authors:
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I Häuser; K Dehesh; K Apel |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Archives of biochemistry and biophysics Volume: 228 ISSN: 0003-9861 ISO Abbreviation: Arch. Biochem. Biophys. Publication Date: 1984 Feb |
Date Detail:
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Created Date: 1984-03-12 Completed Date: 1984-03-12 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0372430 Medline TA: Arch Biochem Biophys Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 577-86 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Cereals
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metabolism* Hordeum / metabolism* Hydrogen-Ion Concentration Light Oxidoreductases / metabolism* Oxidoreductases Acting on CH-CH Group Donors* Temperature Time Factors |
| Chemical | |
Reg. No./Substance:
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EC 1.-/Oxidoreductases; EC 1.3.-/Oxidoreductases Acting on CH-CH Group Donors; EC 1.3.1.33/protochlorophyllide reductase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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