ISSN:
1573-4927
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Abstract Carbonic anhydrase IdMichigan, an electrophoretic variant of human red cell carbonic anhydrase I, was purified from erythrocytes obtained from an individual heterozygous for the trait. Primary structural analysis indicates that a lysine residue has exchanged for a threonine residue in the variant enzyme. After isolation, there was approximately 1.8 times as much normal as variant enzyme. Thermostability studies demonstrated that carbonic anhydrase Id was more thermolabile than the normal enzyme. The normal and variant enzymes showed no differences in specific carboxylesterase activity or CO2 hydratase activity. Utilizing the carboxylesterase activity toward β-naphthyl acetate, the normal and variant enzymes had similar Michaelis constants, pH profiles, and rates of inhibition by acetazolamide. Immunochemical studies did not demonstrate an antigenic difference for the variant enzyme.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00486517
