A 160 kDa protein with carbonic anhydrase activity is complexed with rubisco on the outer surface of thylakoids.
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.
Lazova
Galia N
GN
Institute of Plant Physiology Acad. M Popov, Bulgarian Academy of Sciences, Acad. G Bonchev str. Bl.21, Sofia 1113, Bulgaria. lazova@bio21.bas.bg
Stemler
Alan J
AJ
D002256:Carbonic Anhydrases / Q000737:chemistry / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D007425:Intracellular Membranes / Q000201:enzymology; D008970:Molecular Weight; D018532:Pisum sativum / Q000201:enzymology*; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism*; D012273:Ribulose-Bisphosphate Carboxylase / Q000378:metabolism*; D020524:Thylakoids / Q000201:enzymology*
D010940:Plant Proteins; D012273:Ribulose-Bisphosphate Carboxylase; D002256:Carbonic Anhydrases