Molecular properties of pyrophosphate:Fructose-6-phosphate phosphotransferase from potato tuber

Abstract

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