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From the Department of Microbiology, University of Illinois, Urbana, Illinois 61801 and the Department of Microbiology, Washington University School of Medicine, St. Louis, Missouri 63110
Abstract
Chicken 7S anti-DNP antibodies requiring a high concentration of salt for precipitation with antigen were purified by immunoadsorption. Difference spectra between free and antibody-bound ligand (
-DNP-L-lysine) showed maxima at 392 and 470 nm. These maxima and the 
m at 470 nm were essentially the same as encountered with mammalian and shark antibodies. Chicken anti-DNP antibody of the 7S class has two combining sites (180,000 daltons) as measured in equilibrium dialysis. The average intrinsic association constant (1.6 x 106 M-1 at 5°C) was not altered by wide variation in salt concentration. The 5S bivalent fragment obtained by pepsin digestion also required the anomalous high salt concentration for immune precipitation.
Footnotes
1 This work was supported by United States Public Health Service Grant 5-F2-AI-32,073-02. National Institutes of Health Grants AI-03231 and ST 1 AI-257 and Department of Defense Contract DA-49-193-MD-2330.
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