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Deoxycytidylate antibodies:elicitation, purification and studies on interaction with ligands

Reddy, M and Vijayaraj, * and Jacob, TM (1983) Deoxycytidylate antibodies:elicitation, purification and studies on interaction with ligands. In: Indian Journal of Biochemistry and Biophysics, 20 (6). pp. 321-326.

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To elicit antibodies specific to deoxycytidylate (dpC), rabbits were immunized with dpC conjugates of the carrier proteins bovine serum albumin (BSA) and thyroglobulin (Tg). Antibodies thus formed, when analyzed by Ouchterlony-double diffusion and their binding to [3H]dpC using nitrocellulose filter assay and equilibrium dialysis, showed that the BSA conjugate of dpC is not effective, whereas the Tg conjugate of dpC (Tg-dpC) is effective in eliciting dpC specific antibodies. The antisera raised against Tg-dpC was purified on AH-sepharose-dpC and cellulose-oligo-dpC affinity columns using dpC for elution. Tg-dpC antisera could be separated into 3 fractions, namely, antibodies to Tg, antibodies specific to dpC, and antibodies to the linkage region of the carrier protein and hapten. The affinity constant for the binding of anti-dpC Fab fragments to dpC by equilibrium dialysis was $8.7 \times 10^5 M^{-1}$ at $4^0$ and $1.6 \times 10^5 M^{-1}$ at $32.5^0$. \triangle$H^0$ and \triangle$S^0$ for the binding were -10 kcal/mol and -9 cal/deg/mol, respectively.

Item Type: Journal Article
Publication: Indian Journal of Biochemistry and Biophysics
Publisher: National Institute of Science Communication and Information Resources
Additional Information: Copyright of this article belongs to The Council of Scientific & Industrial Research.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 04 Jul 2008
Last Modified: 27 Aug 2008 13:32
URI: http://eprints.iisc.ac.in/id/eprint/14769

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