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Updated: Jul 6, 2026

Analysis of Thylakoid Membrane Protein Complexes by Blue Native Gel Electrophoresis
Published on: September 28, 2018
A 160 kDa protein with carbonic anhydrase activity is complexed with rubisco on the outer surface of thylakoids
Galia N Lazova1, Alan J Stemler
1Institute of Plant Physiology Acad. M Popov, Bulgarian Academy of Sciences, Acad. G Bonchev str. Bl.21, Sofia 1113, Bulgaria. lazova@bio21.bas.bg
Abstract:
This study provides evidence that, in the soluble fraction from buffer-washed pea thylakoids, one form of soluble carbonic anhydrase (CA) is associated with rubisco in a stromal protein complex. On native-PAGE gels, it is present as a protein band with MW approximately 160 kDa. On SDS-PAGE gels, it is resolved as a single 25-kDa polypeptide. Analysis of Western blots developed with polyclonal antibodies to barley rubisco and to soluble pea CA shows that a 160-kDa protein with CA activity is associated with rubisco in a protein complex localized on the outer surface of thylakoid membranes.
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