Dimethyl sulfoxide favours the covalent phosphorylation and not the binding of Pi to sarcoplasmic reticulum ATPase.
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.
Mintz
E
E
SBPM, Gif-sur-Yvette, France.
Forge
V
V
Guillain
F
F
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
D010710:Phosphates; D015636:Magnesium Chloride; D000252:Calcium-Transporting ATPases; D004121:Dimethyl Sulfoxide