Reactivation of “irreversibly” denaturated enzymes
Open Access
- 1 January 1980
- journal article
- review article
- Published by Wiley in Biotechnology & Bioengineering
- Vol. 22 (1) , 247-251
- https://doi.org/10.1002/bit.260220121
Abstract
No abstract availableThis publication has 14 references indexed in Scilit:
- The principles of enzyme stabilization. III. The effect of the length of intra-molecular cross-linkages on thermostability of enzymesBiochimica et Biophysica Acta (BBA) - Enzymology, 1978
- Enzyme Leakage and Multipoint Attachment of Agarose‐Bound Enzyme PreparationsEuropean Journal of Biochemistry, 1978
- The principles of enzyme stabilizationBiochimica et Biophysica Acta (BBA) - Enzymology, 1977
- The principles of enzyme stabilization I. Increase in thermostability of enzymes covalently bound to a complementary surface of a polymer support in a multipoint fashionBiochimica et Biophysica Acta (BBA) - Enzymology, 1977
- Evidence from rotatory measurements for an intermediate state in the guanidine hydrochloride denaturation of β-lactoglobulinCanadian Journal of Biochemistry, 1977
- Acid induced conformational transition of denatured cytochrome c in urea and guanidine hydrochloride solutionsBiochemistry, 1975
- Experimental and Theoretical Aspects of Protein FoldingAdvances in Protein Chemistry, 1975
- OXIDIZED RNASE AS A PROTEIN MODEL HAVING NO CONTRIBUTION TO THE HYDROGEN EXCHANGE RATE FROM CONFORMATIONAL RESTRICTIONSProceedings of the National Academy of Sciences, 1970
- Proteins as Random Coils. I. Intrinsic Viscosities and Sedimentation Coefficients in Concentrated Guanidine HydrochlorideJournal of the American Chemical Society, 1967
- The denatured states of ribonucleaseJournal of Molecular Biology, 1964