Separation of free and chymotrypsin-bound alpha 2-macroglobulin by affinity chromatography. Its use to demonstrate that the two chymotrypsin-binding sites of alpha 2-macroglobulin are equivalent and independent.
Binary and ternary alpha 2-macroglobulin-chymotrypsin complexes may be quantitatively adsorbed on BH-Sepharose-D-tryptophan methyl ester at pH 8.0 and quantitatively eluted either with acetic acid or with 40% glycerol, pH 8.0. This is the first report of a preparative separation of free and proteinase-bound alpha 2-macroglobulin. Using this affinity chromatographic system, we were able to demonstrate that the two chymotrypsin binding sites of alpha-2-macroglobulin are equivalent and independent.
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002846:Chromatography, Affinity; D002918:Chymotrypsin / Q000302:isolation & purification* / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D046911:Macromolecular Substances; D008433:Mathematics; D011485:Protein Binding; D000511:alpha-Macroglobulins / Q000302:isolation & purification* / Q000378:metabolism
D046911:Macromolecular Substances; D000511:alpha-Macroglobulins; D002918:Chymotrypsin