STRUCTURAL TRANSITIONS IN ANTIBODY AND NORMAL GAMMA-GLOBULINS. 2. FLUORESCENCE POLARIZATION STUDIES
Abstract
The effects of acid, alkali, anionic and cationic detergents, urea and guanidine on the relaxation times of rabbit anti-thyro-globulin antibody and bovine gamma globulin have been evaluated by means of the polarization of fluorescence technique. Both proteins were coupled to dimethylaminonaphthalene sulfonyl chloride. More profound structural modifications occurred in detergent and urea solutions than in acid or basic solutions. However, the effects of alkali persisted even after the globulins had been extensively unfolded by detergents or urea. In contrast to the in dependent action of alkali and the organic reagents, sodium dodecyl sulfate and urea showed interdependent effects. Although the polarization of both protein preparations approached zero in alkali in the presence of either urea or trimethyldodecylammonium chloride the polarizations of the native molecules were regained after neutralization and removal of the reagent by dilution. It would appear that gamma globulins are capable of a continuous unfolding to a state essentially free of noncovalent bonds.
Document Details
- Document Type
- Technical Report
- Publication Date
- Oct 27, 1961
- Accession Number
- AD0407347
Entities
People
- Harold Edelhock
- R. F. Steiner
Organizations
- Naval Medical Research Center