Use of hydrophobic affinity partitioning as a method for studying various conformational states of the human alpha-macroglobulins.
The serum proteins alpha 2-macroglobulin and pregnancy zone protein undergo major conformational changes when complexed with proteinases. It is shown that the changes in delta log Kmax determined by hydrophobic affinity partitioning is a measure of the extent of changes in the conformation of these alpha-macroglobulins. We introduce a new term for the changes of surface hydrophobicity in a protein as delta log Kacc. This defines the difference of delta log Kmax 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.
Jensen
P E
PE
Department of Medical Biochemistry and Biophysics, University of Umeå, Sweden.
Stigbrand
T
T
Shanbhag
V P
VP
D002498:Centrifugation; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002918:Chymotrypsin / Q000378:metabolism; D006801:Humans; D046911:Macromolecular Substances; D008741:Methyl Methanesulfonate / Q000031:analogs & derivatives / Q000494:pharmacology; D008744:Methylamines / Q000494:pharmacology; D011092:Polyethylene Glycols; D011487:Protein Conformation; D000511:alpha-Macroglobulins / Q000737:chemistry*
D046911:Macromolecular Substances; D008744:Methylamines; D000511:alpha-Macroglobulins; C014674:methyl methanethiosulfonate; D011092:Polyethylene Glycols; D008741:Methyl Methanesulfonate; C027451:methylamine; D002918:Chymotrypsin