The renaturation of reduced chymotrypsinogen A in guanidine HCl. Refolding versus aggregation.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference36 articles.
1. Proteins as Random Coils. I. Intrinsic Viscosities and Sedimentation Coefficients in Concentrated Guanidine Hydrochloride
2. The Thermodynamics of Protein Denaturation. II. A Model of Reversible Denaturation and Interpretations Regarding the Stability of Chymotrypsinogen
3. Thermodynamics of protein denaturation. Calorimetric study of the reversible denaturation of chymotrypsinogen and conclusions regarding the accuracy of the two-state approximation
4. THE REVERSIBLE HEAT DENATURATION OF CHYMOTRYPSINOGEN
5. Fragmentation of bovine chymotrypsinogen A and chymotrypsin Aα. Specific cleavage at arginine and methionine residues and separation of peptides, including B and C chains of chymotrypsin
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