## Abstract In pH 5.0–5.4 HAc–NaAc buffer solution, lincomycin (Linco) reacted with Pd(II) to form 1:1 cationic chelate, which could further react with erythrosine (Ery) to form 1:1 ion‐association complexes (Pd–Linco)Ery. As a result, not only were the absorption and fluorescence spectra changed,
Fluorescence studies on interaction between phospho-LHC II and subchloroplast Photosystem 1 preparations
✍ Scribed by Svetlana M. Kochubey; Victor V. Shevchenko; Olga I. Volovik
- Publisher
- Springer
- Year
- 1993
- Tongue
- English
- Weight
- 454 KB
- Volume
- 38
- Category
- Article
- ISSN
- 0166-8595
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✦ Synopsis
Chloroplast proteins were phosphorylated under two test conditions: 'white light' irradiance alone and 'white light' irradiance with the addition of glucose and glucose oxidase, used to produce an anaerobic medium. The interaction of phospho-LHC II with Photosystem 1 (PS 1) was studied for two types of PSI preparation. Changes in the chlorophyll a/b ratio and the ratio of 650 and 680 nm band intensities (E650/E680) in fluorescence excitation spectra were used in calculating the phospho-LHC II portion which became associated with PS 1. It is shown that the associated portion of phospho-LHC II varies for each of the PS 1 preparations and phosphorylation procedures. Possible conclusions as regards the transfer of various sets of LHC II subpopulations under different phosphorylation procedures and the differences of interaction with PS 1 are discussed.
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