Molecular characterization of four forms of phosphofructokinase purified from potato tuber.
Four forms of phosphofructokinase (PFK) have been purified to apparent homogeneity from tubers of potato (Solanum tuberosum cv. Record). Each had a final specific activity of about 200 mumol.min-1.mg-1 protein. Similar forms of PFK were found in partially purified extracts from tubers and leaves of other potato cultivars and related wild species. The relative molecular masses of three forms of PFK were about 200,000 whereas that of the fourth PFK was greater than 800,000. The four forms of PFK contained different proportions of four polypeptides which had apparent relative molecular masses of 46,300, 49,500, 50,000, and 53,000. These polypeptides gave different patterns of peptide fragments after chemical and proteolytic cleavage. Western blots and immunoprecipitation studies using antibodies raised against the individual polypeptides showed that all four are associated with PFK. Thus, potato tubers contain four distinct forms of PFK that differ in their subunit composition.
Kruger
N J
NJ
Biochemistry Department, AFRC Institute of Arable Crops Research, Rothamsted Experimental Station, Harpenden, Herts, United Kingdom.
Hammond
J B
JB
Burrell
M M
MM
D000917:Antibody Formation; D015153:Blotting, Western; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology; D007120:Immunochemistry; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D010447:Peptide Hydrolases; D010455:Peptides / Q000032:analysis; D010732:Phosphofructokinase-1 / Q000276:immunology / Q000302:isolation & purification*; D011198:Solanum tuberosum / Q000201:enzymology*
D010446:Peptide Fragments; D010455:Peptides; D010732:Phosphofructokinase-1; D010447:Peptide Hydrolases