title: Photocleavage of muscle glycogen phosphorylase by vanadate.
abstract: Glycogen phosphorylase is progressively degraded during irradiation with near UV light in the presence of vanadate. The pattern of protein cleavage by monovanadate is characterised by fewer peptides than that by decavanadate, which leads to fragmentation in a ligand dependent way. In both instances, the initial cleavage releases a peptide of 82,000 daltons which accounts for the N-terminal portion of the subunit, including the regulatory phosphorylation site.
authors.affiliation: Istituto di Chimica Biologica dell'Università, Ferrara, Italy.
authors.forename: C M
authors.initials: CM
authors.lastname: Bergamini
authors.forename: M
authors.initials: M
authors.lastname: Signorini
mesh_terms: D001345:Autoradiography; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D006005:Phosphorylases / Q000737:chemistry / Q000378:metabolism* / Q000528:radiation effects; D010766:Phosphorylation; D014466:Ultraviolet Rays; D014638:Vanadates / Q000494:pharmacology*
chemical_list: D014638:Vanadates; D006005:Phosphorylases