Vanadate promotes photooxidative cleavage and inactivation of muscle phosphofructokinase.
During irradiation in the presence of decavanadate, the subunits of phosphofructokinase underwent progressive degradation to a fragment of about 78,000 daltons. This cleavage pattern was altered when the photoirradiation was performed in the presence of monomeric vanadate with formation of several smaller peptides. The specificity of the decavanadate induced cleavage was proved by the resistance of other enzymes to the treatment and by the effects of phosphofructokinase ligands. During irradiation, the activity of the enzyme declined. Differences between the rate of inactivation and of cleavage of enzyme subunits suggest the occurrence of multiple processes.
Signorini
M
M
Istituto di Chimica Biologica dell'Università, Ferrara, Italy.
Bergamini
C M
CM
D000641:Ammonia / Q000494:pharmacology; D000818:Animals; D006868:Hydrolysis; D007700:Kinetics; D008027:Light; D046911:Macromolecular Substances; D009132:Muscles / Q000201:enzymology*; D010446:Peptide Fragments / Q000302:isolation & purification; D010732:Phosphofructokinase-1 / Q000037:antagonists & inhibitors / Q000528:radiation effects*; D010782:Photolysis; D014638:Vanadates / Q000494:pharmacology*
D046911:Macromolecular Substances; D010446:Peptide Fragments; D014638:Vanadates; D000641:Ammonia; D010732:Phosphofructokinase-1