Effects of pressure on sedimentation velocity patterns: I. Alpha chymotrypsin at pH 6.2

Abstract

Computations have been made of possible effects of pressure on the sedimentation of alpha chymotrypsin under previously used experimental conditions, where monomer, dimer, and trimer are in rapid reversible equilibrium. These computations verify a general prediction made earlier, that convective disturbances are to be expected ahead of the moving boundaries when increasing pressure favors the formation of monomer. Moreover, in this case the slow shoulder previously predicted for the pattern in 0.2 ionic strength phosphate buffer at pH 6.2 largely disappears as a result of hydrostatic pressure, affording more satisfactory agreement between predictions and the experimentally observed single symmetrical moving boundary.