Differential Localization of Fraction I Protein between Chloroplast Types | Zendy

Steven C. Huber | Zendy; Timothy C. Hall | Zendy; Gerald E. Edwards | Zendy

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Differential Localization of Fraction I Protein between Chloroplast Types

Author(s) -

Steven C. Huber,

Timothy C. Hall,

Gerald E. Edwards

Publication year - 1976

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.57.5.730

Subject(s) - chloroplast , fraction (chemistry) , differential (mechanical device) , biology , biological system , chemistry , physics , biochemistry , chromatography , gene , thermodynamics

The soluble proteins of C(3) and C(4) mesophyll chloroplasts and C(4) bundle sheath extracts have been analyzed by gel electrophoresis for fraction I protein. Gel scans of soluble protein from C(4) bundle sheath extracts and C(3) mesophyll chloroplasts showed typical fraction I protein peaks that could be identified by ribulose diphosphate carboxylase activity. No such peak was observed for C(4) mesophyll chloroplasts, which also lacked both large and small subunits of ribulose diphosphate carboxylase on sodium dodecyl sulfate gels. The absence of fraction I protein in these chloroplasts was reflected in the soluble protein to chlorophyll ratios, which were roughly 3-fold lower than the ratio obtained for C(3) chloroplasts. The carboxylating enzyme in C(4) mesophyll cells, phosphoenolpyruvate carboxylase, was found to be a major protein in the cytoplasm of C(4) mesophyll protoplasts, and had higher mobility than fraction I protein.

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