ISSN:
1432-2048
Keywords:
Chlorophyll protein complex
;
Photosystem I, II
;
Pisum (thylakoid)
;
Protein kinase
;
Thylakoid fractionation
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract Changes in topography and function of pea (Pisum sativum L.) thylakoid membrane fractions following membrane protein phosphorylation have been studied. After protein phosphorylation the stromal membrane fraction had a higher chlorophyll a/b ratio, an increased content of light-harvesting chlorophyll protein and a higher ratio of chlorophyll to cytochrome f. This indicates that a pool of light-harvesting chlorophyll protein migrates from the photosystem II-enriched grana regions to the photosystem I-enriched stroma lamellae, in agreement with Kyle et al. (1984, Biochim. Biophys. Acta 765, 89–96) and Larsson et al. (1983, Eur. J. Biochem. 136, 25–29). Phosphorylation caused a stimulation in the rate of light-limited photosystem-I electron transfer in the unappressed membrane fraction, indicating that the translocated LHC-II becomes functionally associated with photosystem I.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00392357
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