Effect of calcium ion on the dimerization of alpha-chymotrypsin.
Results of a sedimentation equilibrium study of the inhibitory effect of calcium ion on the dimerization of alpha-chymotrypsin (pH 3.9, I 0.2) are used to establish that the phenomenon does not reflect increased electrostatic repulsion between Ca2(+)-saturated enzyme molecules, but rather the displacement of the monomer-dimer equilibrium by the specific, weak interaction of metal ion with a single site on monomeric enzyme.
Shearwin
K E
KE
Department of Biochemistry, University of Queensland, St. Lucia, Australia.
Winzor
D J
DJ
D002118:Calcium / Q000494:pharmacology*; D002918:Chymotrypsin / Q000378:metabolism; D066298:In Vitro Techniques; D007700:Kinetics; D046911:Macromolecular Substances; D015394:Molecular Structure; D011485:Protein Binding; D014461:Ultracentrifugation
D046911:Macromolecular Substances; D002918:Chymotrypsin; D002118:Calcium