title: The effect of riboflavin binding protein (RPB) on flavokinase catalytic activity.
abstract: 1. Flavokinase isolated from 18-day chick embryo liver shows optimal activity at pH 8.6, in the presence of the divalent cations Zn2+, Ca2+ and Mn2+. 2. The activity and stability of flavokinase depends on the RBP concentration. 3. Interaction between flavokinase and riboflavin binding protein was demonstrated by means of crossed immunoelectrophoresis and affinity chromatography.
authors.affiliation: Institute of Molecular Biology, Jagiellonian University, Krakow, Poland.
authors.forename: M
authors.initials: M
authors.lastname: Słomczynska
authors.forename: Z
authors.initials: Z
authors.lastname: Zak
mesh_terms: D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D002413:Cations, Divalent; D002642:Chick Embryo; D004527:Egg Proteins / Q000378:metabolism*; D004795:Enzyme Stability; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D026901:Membrane Transport Proteins; D010770:Phosphotransferases / Q000302:isolation & purification / Q000378:metabolism*; D017853:Phosphotransferases (Alcohol Group Acceptor)
chemical_list: D002352:Carrier Proteins; D002413:Cations, Divalent; D004527:Egg Proteins; D026901:Membrane Transport Proteins; C019079:riboflavin-binding protein; D010770:Phosphotransferases; D017853:Phosphotransferases (Alcohol Group Acceptor); C022532:riboflavin kinase