Phototransformation of monovinyl and divinyl protochlorophyllide by NADPH:Protochlorophyllide oxidoreductase of barley expressed in Escherichia coli
✍ Scribed by Rosemarie Knaust; Britta Seyfried; Lothar Schmidt; Rüdiger Schulz; Horst Senger
- Book ID
- 103994411
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 653 KB
- Volume
- 20
- Category
- Article
- ISSN
- 1011-1344
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Complementary DNA clones and a corresponding nuclear gene (lpcr) encoding the NADPH-dependent protochlorophyllide oxidoreductase (pchlide reductase, EC 1.6.99.1) have been characterized from pea (Pisum sativum L.). The pea lpcr gene encodes a 43 118 Da precursor polypeptide comprised of a transit pe
In etiolated barley (Hordeum vulgare L.) seedlings the light-induced accumulation of chlorophyll is controlled by two light-dependent NADPH-protochlorophyllide oxidoreductase (POR; EC 1.6.99.1) enzymes. While the concentration of one of these enzymes (POR A) and its mRNA rapidly decline during illum