Evidence of a biotin dependent acetyl-coenzyme A carboxylase in rat muscle.
Rat hindlimb muscle tissue was extracted from male Sprague-Dawley rats exsanguinated under light ether anesthesia. Muscle homogenates (50,000 x g supernatant) were incubated with ATP, bicarbonate, acetyl-CoA, and citrate. The quantity of malonyl-CoA synthesized was determined by malonyl-CoA incorporation into long acyl chains using tritiated acetyl-CoA and fatty acid synthetase. Malonyl-CoA synthesis was found to be dependent on the presence of ATP, bicarbonate, citrate, and acetyl-CoA in the incubation medium. Incubation with avidin showed near complete inhibition of carboxylation that was restored with the addition of biotin. These results represent strong evidence of a biotin containing acetyl-CoA carboxylase in skeletal muscle.
Departments of Biochemistry, Brigham Young University, Provo, Utah 84602.
G E
GE
Trumble
M A
MA
Smith
W W
WW
Winder
D000103:Acetyl-CoA Carboxylase / Q000378:metabolism*; D000818:Animals; D001360:Avidin / Q000378:metabolism; D001710:Biotin / Q000378:metabolism*; D008297:Male; D008316:Malonyl Coenzyme A / Q000096:biosynthesis / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D013379:Substrate Specificity
D001360:Avidin; D008316:Malonyl Coenzyme A; D001710:Biotin; D000103:Acetyl-CoA Carboxylase