title: Dimethyl sulfoxide favours the covalent phosphorylation and not the binding of Pi to sarcoplasmic reticulum ATPase.
abstract: Competition between Ca2+ binding and Pi phosphorylation showed that the affinity of Ca(2+)-ATPase for Pi was not changed by 20% DMSO. Thus, the enhancement of Pi phosphorylation in the presence of DMSO should not be attributed to a solvent effect on the affinity for Pi, but rather on the phosphorylation reaction itself.
authors.affiliation: SBPM, Gif-sur-Yvette, France.
authors.forename: E
authors.initials: E
authors.lastname: Mintz
authors.forename: V
authors.initials: V
authors.lastname: Forge
authors.forename: F
authors.initials: F
authors.lastname: Guillain
mesh_terms: D000818:Animals; D001665:Binding Sites; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D004121:Dimethyl Sulfoxide / Q000494:pharmacology*; D015636:Magnesium Chloride / Q000378:metabolism; D010710:Phosphates / Q000378:metabolism*; D010766:Phosphorylation / Q000187:drug effects; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000187:drug effects* / Q000201:enzymology
chemical_list: D010710:Phosphates; D015636:Magnesium Chloride; D000252:Calcium-Transporting ATPases; D004121:Dimethyl Sulfoxide