Rat liver microsomal palmitoyl-CoA synthetase: subunit structure.
Long chain fatty acyl-CoA synthetase (acid:CoA ligase (AMP-forming), EC 6.2.1.3) from rat liver microsomes was shown to dissociate completely into one polypeptide chain in 75% 2-chloroethanol in water. The presence of one amino and one carboxy terminal was established. The molecular weight of the subunit as deduced from sedimentation equilibrium as well as quantitative carboxy terminal analysis agrees with the value of 28 000 +/- 1000 as reported previously (Bar-Tana, J. and Rose, G. (1973) Biochem. J. 131, 443--449). Hence, the catalytic unit of 168 000 daltons appears to be composed of identical subunits.
D000818:Animals; D003066:Coenzyme A Ligases / Q000032:analysis*; D005023:Ethylene Chlorohydrin; D008862:Microsomes, Liver / Q000201:enzymology*; D008970:Molecular Weight; D011487:Protein Conformation; D051381:Rats
D005023:Ethylene Chlorohydrin; D003066:Coenzyme A Ligases