Reddy, Vijayaraj M and Jacob, TM (1983) Antibodies to dpApT sequence: purification and studies on their specificity and affinity to different ligands. In: Indian Journal of Biochemistry & Biophysics, 20 (4). pp. 183-187.Full text not available from this repository. (Request a copy)
Antibodies specific to the dinucleotide, dpApT, were elicited in rabbits using a thyroglobulin (Tg) conjugate of dpApT(Tg-dpApT) as the immunogen. The dpApT antibodies were isolated from anti-Tg-dpApT \gamma-globulins by adsorption to an AH-Sepharose-dpApT affinity column and elution with 0.1N HOAc and were further purified using an AH-Sepharose-dpC column. The specificity and affinity of purified dpApT antibodies were analyzed by the inhibition of the binding of [3H]dpApT as well as denatured [32P]DNA to the antibodies with various nonradioactive nucleotides and their derivs. The antibodies were sequence-specific. Their binding to denatured DNA was poorly inhibited by deoxynucleoside 5'-monophosphates as compared to dpApT whereas DNAs from varying sources were inhibitory to different extents. The affinity consts. for the binding of [3H]dpApT to the antibodies as detd. by equil. dialysis were $9.6_x$ 106M-1 at $14^o$ and $2.3_x$106M-1 at $32.5^o$; \Delta$H^o$ and \Delta$S^o$ for the binding were -13.4 kcal/mol and -14.8 cal/deg/mol, resp.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to NISCAIR.|
|Department/Centre:||Division of Biological Sciences > Biochemistry|
|Date Deposited:||14 Jul 2008|
|Last Modified:||27 Aug 2008 13:35|
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