Spectroscopic characterizations of alpha feto protein binding with its antibody by irma method in tissue’s homogenate of some types of ovarian tumors

Abstract EN

Spectroscopic studies, in the ultraviolet region were carried out to characterize the binding of isolated AFP with its labeled antibody in human malignant germ cell ovaria, tumor homogenates.

Factors affecting the absorption properties of AFP, and the complex of isolated AFP with the labeled antibody such as pH, solvent polarity (solvent perturbation technique), spectrophotometric pH titration and thermal stability in the presence of different concentration of sodium chloride have been studied.

The spectroscopic pH titration curves for human AFP and for the complex of isolated AFP with the labeled antibody gave pka of 5.

7 and 7.

3 for histidine residue, respectively, while 11.

6 and 11.

4 for tyrosine residue, respectively.

Furthermore the study showed that 23.

8 % of histidine and 70.

4 % of tyrosine residue are located on the surface of human AFP antigen, while these residues were located 38.

0 % and 31.

0 % on the surface of complex of the isolated AFP form.