Studies on the Denaturation of Taka-amylase A and on Its Reversibility
- 1 November 1962
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 52 (5) , 314-323
- https://doi.org/10.1093/oxfordjournals.jbchem.a127622
Abstract
Incubation in 8 [image]urea-0.01 [image]ethylenediaminetetraacetate at pH 6-8 completely denatured the enzyme. The enzyme was reactivated at pH 8.5(opt. pH) by diluting or dialyzing out urea. The denaturation was more effective at lower enzyme concentrations and lower ionic strengths.Keywords
This publication has 3 references indexed in Scilit:
- REGENERATION OF NATIVE SECONDARY AND TERTIARY STRUCTURES BY AIR OXIDATION OF REDUCED RIBONUCLEASE1961
- The Amino Acid Composition of α-Amylase from Aspergillus oryzaeJournal of Biological Chemistry, 1960
- On the N-Terminal Peptide of Taka-Amylase AThe Journal of Biochemistry, 1959