Evidence from gel filtration and sedimentation studies of crystalline bovine liver rhodanese indicated that the enzyme molecule of 37,000 molecular weight is a dimer. In the native state, this form is in rapid, pH-dependent equilibrium with the monomeric species. A stable dimer is formed under mild oxidizing conditions. Analysis of the protein by peptide mapping indicated that the monomers are identical. Polarographic analysis for metal ions showed that the enzyme contains 1 zinc ion per monomer.
No takes yet. Share an insight, caveat, or question.
Volini et al. (1967) studied this question.
Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context: