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Abstract
1 Methylmalonyl-CoA mutase from Propionibacterium shermanii has been purified according to a modification of the method described by Wood et al. in 1964. 2 The final mutase preparation was homogeneous in the ultracentrifuge showing the following hydrodynamic properties: 8020,W= 7.25 S, D020,w= 5.71 F. Its molecular weight was calculated to be 124000. A similar molecular weight was indicated also by gel-filtration on a calibrated Sephadex G-100 column both for the mutase apo-enzyme and the hydroxycob(III)alamin · mutase complex. 3 On treatment with guanidine hydrochloride methylmalonyl-CoA mutase dissociates into two polypeptide chains, which are similar, though not identical in size. Dodecylsulphate electrophoresis indicated for the molecular weights of the two polypeptide chains 61000 7plusmn; 3000 and 66000 ± 3000, respectively. 4 In the presence of excess hydroxycob(III)alamin methylmalonyl-CoA mutase was crystallised as pink needles consisting of the enzymically inactive inhibitor · protein complex.
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