Hybridization of Half Molecules of Rabbit Gamma Globulin
- 24 January 1964
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 143 (3604), 376-379
- https://doi.org/10.1126/science.143.3604.376
Abstract
Specifically purified rabbit antiovalbumin and normal γ-globulin labeled with 1-131 were dissociated into half molecules by reduction and acidification. When a mixture of the two preparations was neutralized, a large proportion of mixed molecules having active combining sites and the same sedimentation coefficient as the original γ-globulins was formed. Since the sulfhydryl groups were inactivated after reduction, the recombined subunits appear to be linked by noncovalent bonds.Keywords
This publication has 10 references indexed in Scilit:
- Reduction and Reoxidation of a Critical Disulfide Bond in the Rabbit Antibody MoleculePublished by Elsevier ,1963
- Effect of Reduction of Several Disulfide Bonds on the Properties and Recombination of Univalent Fragments of Rabbit AntibodyJournal of Biological Chemistry, 1963
- Quantitative Estimation of the Hybridization of Rabbit AntibodiesNature, 1962
- REDUCTION OF GAMMA-GLOBULINS1962
- Recombination of Univalent Subunits Derived from Rabbit AntibodyJournal of Biological Chemistry, 1961
- STRUCTURAL DIFFERENCES AMONG ANTIBODIES OF DIFFERENT SPECIFICITIESProceedings of the National Academy of Sciences, 1961
- Recombination of a mixture of univalent antibody fragments of different specificityArchives of Biochemistry and Biophysics, 1961
- STUDIES ON STRUCTURAL UNITS OF THE γ-GLOBULINSThe Journal of Experimental Medicine, 1961
- A Simple Chromatographic Method for Preparation of Gamma Globulin.Experimental Biology and Medicine, 1960
- The serum proteins in multiple myelomatosisBiochemical Journal, 1940