Effect of cadmium acetate on the conformation of lysozyme: functional implications.
Structural variations of lysozyme as a consequence of its interaction with CdAc2, as well as the implications on the protein functionality have been studied. Variations in the conformation of the macromolecule are seen, however these changes are not reflected on the secondary structure. The interaction of the salt with the polypeptide chain is weak and thermodynamically unfavourable. Molecular aggregates (dimer forms) are observed at the highest salt concentrations. This interaction causes an inhibitory effect on lysozyme, the activity loss being 50% at the highest salt concentration studied. The inhibition is of mixed type with an uncompetitive component. Thus cadmium does not bind to the active site of the enzyme which is in accordance with the not very large activity loss observed. The substrate inhibition of lysozyme is favoured in the presence of the salt, so interaction with the macromolecule is at low affinity sites.
Olmo
R
R
Departamento de Bioquímica y Biología Molecular, Facultad de Medicina, Universidad Complutense de Madrid, Spain.
Blanco
M D
MD
Socorro
J M
JM
Martín
J A
JA
Teijón
J M
JM
D000085:Acetates / Q000494:pharmacology*; D002104:Cadmium / Q000494:pharmacology*; D002850:Chromatography, Gel; D002942:Circular Dichroism; D003720:Densitometry; D009113:Muramidase / Q000737:chemistry* / Q000187:drug effects* / Q000378:metabolism; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet
D000085:Acetates; D002104:Cadmium; C028031:cadmium acetate; D009113:Muramidase