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Immunological distinction between fraction I protein and protochlorophyllide holochrome.
Author(s) -
Rodney H. Falk,
Lawrence Bogorad
Publication year - 1969
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.44.12.1669
Subject(s) - protochlorophyllide , etiolation , biochemistry , sedimentation coefficient , chemistry , fraction (chemistry) , pyruvate carboxylase , enzyme , biology , chromatography , biosynthesis
Ribulose 1,5-diphosphate carboxylase (RuDP carboxylase) has been shown to be the major component of the Fraction I protein of leaves (5,6). Protochlorophyllide associated with a protein, i.e. protochlorophyllide holochrome (PCH), has been isolated from etiolated bean leaves (1,9,10); upon illumination in vivo or in vitro it is transformed into chlorophyllide holochrome. Several investigators (1,4, 10) have been unsuccessful in their attempts to separate RuDP carboxylase from PCH and consequently have suggested that the proteins might be identical on the basis of their correspondence with regard to sedimentation velocity, molecular weight and diffusion coefficient.

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