An ADPase from sarcoplasmic reticulum of rabbit muscle cleaves ADP bound to F-actin.
We have found that sarcoplasmic reticulum from rabbit muscle contains an ADPase which cleaves ADP bound to F-actin. The interaction is not of the simple Michaelis-Menten type, the order of the reaction being larger than the first. A possible explanation of this behaviour could be that ADPase binds to two adjacent actin monomers with a preferred orientation thus cleaving preferentially the nucleotide of one of the two monomers.
D000199:Actins / Q000378:metabolism*; D000244:Adenosine Diphosphate / Q000378:metabolism*; D000818:Animals; D001081:Apyrase / Q000378:metabolism*; D007700:Kinetics; D009132:Muscles / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*; D013379:Substrate Specificity
D000199:Actins; D000244:Adenosine Diphosphate; D010744:Phosphoric Monoester Hydrolases; D001081:Apyrase