Influence of subunit interaction and intersubunit disulphide bonds on the unfolding of immunoglobulin G by guanidine hydrochloride
- 21 September 1973
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure
- Vol. 322 (1) , 45-52
- https://doi.org/10.1016/0005-2795(73)90173-6
Abstract
No abstract availableThis publication has 11 references indexed in Scilit:
- Recovery of the native conformations of the variable and constant halves of an immunoglobulin light chain upon renaturation from the linear random coil stateImmunochemistry, 1972
- Properties of the Fd fragment from rabbit immunoglobulin GBiochemistry, 1972
- Conformational changes accompanying the dissociation and association of immunoglobulin-G subunitsBiochimica et Biophysica Acta (BBA) - Protein Structure, 1972
- Denaturation of globular proteins by guanidine thiocyanate I. Optical rotation in aqueous guanidine thiocyanate solutionsBiochimica et Biophysica Acta (BBA) - Protein Structure, 1971
- Recovery of native conformation of rabbit immunoglobulin G upon recombination of separately renatured heavy and light chains at near-neutral pHBiochemistry, 1971
- Gross conformation of free polypeptide chains from rabbit immunoglobulin G. I. Heavy chainBiochemistry, 1971
- The recombination of dimers of immunoglobulin peptide chainsBiochemical Journal, 1970
- Molecular Size and Conformation of ImmunoglobulinsPublished by Elsevier ,1970
- Protein DenaturationAdvances in Protein Chemistry, 1968
- THE ROLE OF DISULFIDE BONDS IN THE COMPLEMENT-FIXING AND PRECIPITATING PROPERTIES OF 7S RABBIT AND SHEEP ANTIBODIESThe Journal of Experimental Medicine, 1964