Purification and partial characterization of 200 kDa oncofetal antigen from radiation induced murine lymphocytic lymphoma.
1. A 200 kDa glycoprotein (gp200) oncofetal antigen was purified from solubilized membranes of a radiation-induced murine lymphocytic lymphoma cell line (XR11-5T), grown in syngeneic RFM mice, by successive gel chromatography of the active fraction on lentil lectin agarose, Q- and S-Sepharose and Superose-12 using an FPLC system. 2. A murine monoclonal antibody 115, produced by the syngeneic immunization of adult male C57BL/6N mice with 12-day mouse fetal cells, was used in a slot blot antibody assay to follow up the active fractions. 3. The purified glycoprotein has a pI of 5. 4. 4. Treatment of radiolabeled gp200 with neuraminidase caused a slight reduction in size due to the removal of sialic acid groups and a shift in pI to 6. 3. 5. Treatment of gp200 with different glycosidases shows that gp200 is susceptible to N- and O-glycanase but not to endoglycosaminidase H. 6. On extraction of gp200 with Triton X-114 it partitions exclusively into the detergent-rich fraction consistent with being an integral membrane protein.[1]References
- Purification and partial characterization of 200 kDa oncofetal antigen from radiation induced murine lymphocytic lymphoma. Barsoum, A.L., Coggin, J.H. Int. J. Biochem. (1993) [Pubmed]
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