Denaturation and renaturation of the monomeric phosphoglycerate mutase from Schizosaccharomyces pombe.
The denaturation by guanidinium chloride of the monomeric phosphoglycerate mutase from Schizosaccharomyces pombe was studied. The loss in activity broadly parallels the changes in protein structure detected by fluorescence and c.d. Renaturation can be brought about by dilution of the denaturing agent. These processes were compared with those in the enzymes from baker's yeast and rabbit muscle, which are tetrameric and dimeric respectively. The effects of the cofactor 2,3-bisphosphoglycerate on the structure and stability of the S. pombe enzyme were also investigated.
Johnson
C M
CM
Department of Biological Science, University of Stirling, Scotland, U.K.
Price
N C
NC
D002942:Circular Dichroism; D010450:Endopeptidases; D019791:Guanidine; D006146:Guanidines; D010736:Phosphoglycerate Mutase; D010770:Phosphotransferases; D011489:Protein Denaturation / Q000187:drug effects; D012440:Saccharomyces / Q000201:enzymology*; D013050:Spectrometry, Fluorescence
D006146:Guanidines; D010770:Phosphotransferases; D010450:Endopeptidases; D010736:Phosphoglycerate Mutase; D019791:Guanidine