Abstract
The inner etioplast membrane possesses a pronounced lateral heterogeneity with respect to protein and lipid composition as well as ultrastructural appearance. Little is known about the reason for formation of the regular branched structure shown by the prolamellar body part of the membrane. A specific interaction between the membrane lipids and the dominating protein NADPH‐protochlorophyllide oxidoreductase (PCR, EC 1.6.99.1) might be of major importance. In this study isolated prolamellar bodies and prothylakoids from the leaves of dark‐grown wheat (Triticum aestivum L. cv. Starke II, Weibull) were exposed to Triton X‐114 partitioning in media with 150 mM NaCl and without. By comparing the partitioning of PCR, the ATP synthase (EC 3.6.1.3) polypeptides, and ribulosebisphosphate carboxylaseoxygenase (EC 4.1.1.39) in the different systems, it was concluded that PCR is an integral membrane protein with substantial hydrophilic domains.
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Dates
Type | When |
---|---|
Created | 19 years, 4 months ago (April 30, 2006, 10:04 p.m.) |
Deposited | 1 year, 10 months ago (Oct. 22, 2023, 7:45 a.m.) |
Indexed | 3 weeks, 6 days ago (Aug. 5, 2025, 8:10 a.m.) |
Issued | 35 years, 10 months ago (Nov. 1, 1989) |
Published | 35 years, 10 months ago (Nov. 1, 1989) |
Published Online | 19 years, 4 months ago (April 28, 2006) |
Published Print | 35 years, 10 months ago (Nov. 1, 1989) |
@article{Selstam_1989, title={Hydrophobicity of protochlorophyllide oxidoreductase, characterized by means of Triton X‐114 partitioning of isolated etioplast membrane fractions}, volume={77}, ISSN={1399-3054}, url={http://dx.doi.org/10.1111/j.1399-3054.1989.tb05660.x}, DOI={10.1111/j.1399-3054.1989.tb05660.x}, number={3}, journal={Physiologia Plantarum}, publisher={Wiley}, author={Selstam, Eva and Widell‐Wigge, Anna}, year={1989}, month=nov, pages={401–406} }