Abstract
The serum proteins α 2-macroglobulin and pregnancy zone protein undergo major conformational changes when complexed with proteinases. It is shown that the changes in Δlog K max determined by hydrophobic affinity partitioning is a measure of the extent of changes in the conformation of these α-macroglobulins. We introduce a new term for the changes of surface hydrophobicity in a protein as Δlog K acc. This defines the difference of Δlog K max between a modified and an unmodified conformational state of a specific protein and can be useful as a parameter to describe the apparent conformational changes in the protein.
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