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Identification of chloroplast thylakoid membrane polypeptides: Coupling factor of photophosphorylation (CF 1 ) and cytochrome f
Author(s) -
Süss K.-H.
Publication year - 1976
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(76)80755-7
Subject(s) - photophosphorylation , thylakoid , coupling (piping) , plastocyanin , chemistry , electron transport chain , chloroplast , physics , biochemistry , photosystem i , gene , mechanical engineering , engineering
Recently much information has become available concerning the polypeptide composition of chloroplast thylakoid membranes from many sources using different sodium dodecyl sulfate (SDS)-acrylamide-gel electrophoresis systems [ 1,2] . From all electrophoretical resolved membrane polypeptides only the pigment-protein complexes I and II [ 1,2] and the LY and fl subunits of CFr [3] have been clearly identified in the polypeptide profiles. The nature of the other polypeptides which are subunits of associated proteins [4] is questionable. If the gel electrophoresis is used as a tool in the study of structure-function relationships of photosynthetic membranes their identification becomes necessary. This paper presents data on the characterization of purified cytochrome f and coupling factor (CFr ). For the identification of the polypeptides of these proteins in the membrane polypeptide spectra their electrophoretic mobilities were examined after separation on two different gel systems. It was found that four subunits of CFr (u.J,-y,e) and the subunit of cytochrome fare equivalent to distinct peaks in the membrane polypeptide profiles.