Cystic fibrosis alpha 2-macroglobulin protease interaction in vitro.
alpha 2-Macroglobulin was purified from plasma of five cystic fibrosis patients and five normal controls. SDS gel electrophoresis of native alpha 2-macroglobulin from cystic fibrosis patients and normal donors showed identical subunit molecular weights, as did trypsin cleavage products. Cystic fibrosis and control alpha 2-macroglobulins were indistinguishable by isoelectric focusing and exhibited appropriate shifts in isoelectric point following binding of trypsin. The trypsin-binding capacities of control and cystic fibrosis alpha 2-macroglobulins did not differ, nor did the esterolytic activity of the trypsin-alpha 2-macroglobulin complexes.
D000293:Adolescent; D000328:Adult; D003550:Cystic Fibrosis / Q000097:blood* / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D066298:In Vitro Techniques; D007525:Isoelectric Focusing; D008297:Male; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000097:blood / Q000378:metabolism; D011480:Protease Inhibitors / Q000378:metabolism; D011485:Protein Binding; D014357:Trypsin / Q000378:metabolism*; D000511:alpha-Macroglobulins / Q000302:isolation & purification / Q000378:metabolism*
D011480:Protease Inhibitors; D000511:alpha-Macroglobulins; D010447:Peptide Hydrolases; D014357:Trypsin