Abstract
Limited proteolysis of barley ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBPCO) was effected by treatments with trypsin and Staphylococcus aureus strain V8 protease. Treatment of native RuBPCO with proteases resulted in the degradation of the large subunit (LS) of the enzyme. Trypsin cleaved three fragments from the LS but the S. aureus strain V8 protease cleaved only one. The small subunit (SS) was not affected. In the presence of 0.5 % sodium dodecyl sulfate, RuBPCO degraded into several fragments; some of them were fairly stable. Monoclonal antibodies (Mabs) against barley RuBPCO were applied in immunoblotting analysis to distinguish which of the fragments were recognized. All the Mabs recognized the fragments with molecular masses close to those of the LS. Differences among Mabs were observed in the fragments with low molecular mass.
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Demirevska-Kepova, K., Simova-Stoilova, L. & Kyurkchiev, S. Proteolytic degradation of barley ribulose-1,5-bisphosphate carboxylase/oxygenase and recognition of the fragments by monoclonal antibodies. Photosynthetica 34, 211–218 (1998). https://doi.org/10.1023/A:1006888506925
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DOI: https://doi.org/10.1023/A:1006888506925