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. 1989 Jun 1;260(2):353–358. doi: 10.1042/bj2600353

Subunit interactions in Propionibacterium shermanii methylmalonyl-CoA mutase studied by analytical ultracentrifugation.

E N Marsh 1, S E Harding 1, P F Leadlay 1
PMCID: PMC1138676  PMID: 2569862

Abstract

The effect of increasing ionic strength on adenosylcobalamin-dependent methylmalonyl-CoA mutase from Propionibacterium shermanii was studied by using analytical ultracentrifugation. Both sedimentation-velocity and low-speed sedimentation-equilibration measurements show that the enzyme dissociates progressively into its two dissimilar subunits with increasing ionic strength. Equilibrium between the alpha beta-dimer and the separated subunits is rapidly established under these conditions. Dissociation is accompanied by loss of enzymic activity, but the position of the equilibrium is unaffected by the presence of either substrate or adenosylcobalamin cofactor.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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