Purification and properties of adenosine deaminase in normal and hereditary hemolytic anemia with increased red cell activity.
Red cell adenosine deaminase from normal subjects and from a patient with hereditary hemolytic anemia with a 40-fold increase in activity were purified using antibody affinity chromatography. The purified enzymes were completely homogeneous on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. There were no differences in the molecular weight, specific activity, polyacrylamide gel electrophoresis, Michaelis constant for adenosine, inhibition constant for guanylurea, utilization of 2-deoxyadenosine, thermal stability, optimum pH, immunological reactivity, amino acid composition and tryptic peptide mapping. These results strongly suggest that increased red cell adenosine deaminase activity is caused by an overproduction of a structurally normal enzyme.
D000243:Adenosine Deaminase / Q000097:blood* / Q000302:isolation & purification; D000596:Amino Acids / Q000032:analysis; D000743:Anemia, Hemolytic / Q000201:enzymology* / Q000235:genetics; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D007700:Kinetics; D009700:Nucleoside Deaminases / Q000097:blood*; D010446:Peptide Fragments / Q000032:analysis; D014357:Trypsin
D000596:Amino Acids; D010446:Peptide Fragments; D014357:Trypsin; D009700:Nucleoside Deaminases; D000243:Adenosine Deaminase