Mar 11, 1976

A study of the single polypeptide nature of rhodanese. A comparison of different preparations

Biochimica Et Biophysica Acta
J M Crawford, P M Horowitz

Abstract

The enzyme rhodanese (EC 2.8.1.1) appears as a single polypeptide chain protein on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The molecular weight of this species is approx. 33 000. This contrasts with previous reports that rhodanese behaves on gel filtration chromatography as a rapidly equilibrating monomer-dimer system composed of identical subunits with a molecular weight of 18 500. We have investigated this apparent discrepancy by isolating the enzyme by the two different preparative procedures used in the above investigations. The two crystalline samples were subjected to gel filtration chromatography under a wide variety of conditions and to sodium dodecyl sulfate disc gel electrophoresis. The two preparations yielded rhodanese which behaved identically and no evidence for the monomeric species was obtained under any experimental condition tested. Thin-layer gel chromatography of clarified liver homogenates gave no evidence of rhodanese species other than that present in the purified samples. The variation in molecular weights observed in gel filtration chromatography may be a reflection of the conformational mobility of the enzyme leading to solvent-dependent changes in Stokes radius. If rhodanese is dime...Continue Reading

  • References1
  • Citations8

References

  • References1
  • Citations8

Citations

Mentioned in this Paper

Macromolecular Compounds
Sulfurtransferase
Electrophoresis, Disc
Irium
Bos indicus
Molecular Sieve Chromatography
Hydrogen-Ion Concentration
Metazoa
TST
Liver

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