The denaturation of covalently inhibited swine pepsin.
International journal of peptide and protein research
confidence
Key findings
Denaturation studies of covalently inhibited swine pepsin; no clinical or biological endpoints reported.
View source on PubMed (PMID 29843) ↗
- Sample size
- Not reported
- Population
- In vitro swine pepsin (enzyme)
- Dosing
- Diazoacetylglycine ethyl ester to inactivate pepsin; varying pH and guanidine hydrochloride concentrations
- Duration
- Not reported
- Route
- In vitro
- Blinding
- not_reported
- Controls
- not_reported
- Drug class
- digestive enzyme blend
Full abstract
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.