The denaturation of covalently inhibited swine pepsin

Int J Pept Protein Res. 1978 Sep;12(3):155-63. doi: 10.1111/j.1399-3011.1978.tb02879.x.


Studies are reported on the denaturation of freshly prepared, intact swine pepsin, which was inactivated by reaction with diazoacetylglycine ethyl ester, to prevent autolysis. Denaturation about pH 6 was found to involve a small expansion of the molecular domain with some loss of organized secondary structure. On the other hand, increasing concentrations of guanidine hydrochloride induced cooperative transitions in both the native and alkali denatured forms to give a cross-linked random coil. No conditions could be found in which these reactions were reversible. Removal of denaturing conditions usually resulted in aggregation and precipitation of protein. From these studies, it would seem that the active conformation is largely predetermined in the zymogen.

MeSH terms

  • Animals
  • Autolysis
  • Circular Dichroism
  • Hydrogen-Ion Concentration
  • Indicators and Reagents
  • Pepsin A*
  • Protein Conformation*
  • Protein Denaturation
  • Spectrum Analysis
  • Swine
  • Viscosity


  • Indicators and Reagents
  • Pepsin A