title: ATP binding to bovine serum albumin.
abstract: Specific binding of ATP to bovine serum albumin (BSA) is demonstrated employing ATP derivatives spin-labeled at either N6 or C8 of adenine ring or at the ribose moiety. Based on a 1:1 stoichiometry binding constants are in the 50-100 microM range. Binding is largely competitive with ATP or stearic acid. A small fraction of the labeled nucleotides could not be liberated by these ligands. Binding of AMP is in the millimolar range, only.
authors.affiliation: Fachbereich Chemie, Universität Kaiserslautern, Germany.
authors.forename: M
authors.initials: M
authors.lastname: Bauer
authors.forename: J
authors.initials: J
authors.lastname: Baumann
authors.forename: W E
authors.initials: WE
authors.lastname: Trommer
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D066298:In Vitro Techniques; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*
chemical_list: D012710:Serum Albumin, Bovine; D000255:Adenosine Triphosphate