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ELECTROPHORETIC AND SPECTROPHOTOMETRIC STUDIES OF CHLOROPHYLL‐PROTEIN COMPLEXES FROM TOBACCO CHLOROPLASTS. ISOLATION OF A LIGHT HARVESTING PIGMENT PROTEIN COMPLEX WITH A MOLECULAR WEIGHT OF 70,000
Author(s) -
Remy R.,
Hoarau J.,
Leclerc J. C.
Publication year - 1977
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1977.tb07466.x
Subject(s) - chloroplast , chlorophyll , thylakoid , electrophoresis , p700 , chlorophyll a , pigment , protein subunit , polyacrylamide gel electrophoresis , chemistry , molecular mass , gel electrophoresis , biochemistry , chromatography , photosystem i , organic chemistry , enzyme , gene
— …After a short‐term solubilization with sodium dodecyl sulphate, chloroplast membranes of tobacco were separated by polyacrylamide gel electrophoresis into three chlorophyll‐protein complexes. In addition to the two major complexes termed I and II c corresponding respectively to P700 chlorophyll a ‐protein and light‐harvesting chlorophyll a/b ‐protein described by Thornber (1975), a relatively stable complex termed II a has been observed. This new complex has an apparent molecular weight of 70,000 daltons and possesses Chl a and b. Complexes I, II a and II C have been isolated and precise spectroscopic analyses have been performed. Fourth derivative analyses of low temperature absorption spectra suggest that complex II a seems more representative than II C of chlorophyll a forms present in intact thylakoid membranes. Moreover, the electrophoretic study reveals that CP I and CP II are composed of only one polypeptidic subunit with respective molecular weights of 68,000 and 24,000 daltons.