Abstract
Alpha Fetoprotein (AFP) is a major serum protein in the developing fetus and is of clinical significance as it is an oncofetal protein being synthesized by fetal organs and malignant tumors. AFP is here used as a diagnostic marker for hepatic carcinomas. In view of structural homology and similarities in physico-chemical properties with serum albumin, the separation and purification of AFP has always been a problem. Immunologically active AFP has been purified from human cord plasma using pseudoaffinity chromatography based on Cibacron blue substituted Sephadex G-100. AFP was quantified using rocket immunoelectrophoresis and double sandwich ELISA. Polyclonal antibodies were raised against purified AFP in mice. The purified antibodies were conjugated with peroxidase for use in double antibody sandwich ELISA. Purification of AFP from human cord plasma by an improved method with 55% recovery is reported.
Published Version
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