Characterization of reactivation produces from human carbonic anhydrase I denatured in various concentrations of guanidine hydrochloride.
Denaturation in 1.7 M guanidine hydrochloride (Gnd-HCl), thermostability tests, immunological tests and polyacrylamide-gel electrophoresis were performed on the products of reactivation from human carbonic anhydrase I (CA I), initially denatured in various concentrations of Gnd-HCl. Reactivated protein from CA I denatured in 2 M Gnd-HCl exhibited different thermostability and immunological properties from the products of other Gnd-HCl concentrations. The CA I denatured in 2 M Gnd-HCl was found to be more heat stable and achieved complete inhibition at an antibody concentration one-fourth that of the other Gnd-HCl denaturation concentrations. These data suggest that 2 M Gnd-HCl produces a reactivation product with a different tertiary structure from 5 M or 0.5 M Gnd-HCl.
D002256:Carbonic Anhydrases / Q000378:metabolism*; D004355:Drug Stability; D004591:Electrophoresis, Polyacrylamide Gel; D006146:Guanidines / Q000494:pharmacology*; D006801:Humans; D007527:Isoenzymes / Q000378:metabolism; D007700:Kinetics; D011489:Protein Denaturation; D013696:Temperature
D006146:Guanidines; D007527:Isoenzymes; D002256:Carbonic Anhydrases