Molecular properties of pyrophosphate:Fructose-6-phosphate phosphotransferase from potato tuber
作者： Nicholas J. Kruger , David T. Dennis
DOI: 10.1016/0003-9861(87)90446-2
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摘要: Pyrophosphate:fructose-6-phosphate phosphotransferase (PFP) from potato tubers has been purified to homogeneity. The enzyme contains two polypeptides with apparent relative molecular mass (Mr) values of 65,000 and 60,000. These give different peptide fragments after limited proteolytic digestion. Antibodies raised against each polypeptide separately are specific for that polypeptide, but both antisera capable immunoprecipitating native PFP activity. antibodies also recognize similar pairs in a range other plant tissues contain Based on gel filtration, the Mr value tuber is 265,000. This suggests heterotetramer composed In presence pyrophosphate, dissociates into 130,000 dimer.
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