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Tumor-associated changes in plasma samples revealed by two-dimensional macromolecular mapping and selective lectin binding.

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Two-dimensional electrophoretic analysis of plasma samples from EL-4 lymphoma-bearing C57 black mice revealed five 75 kd protein species in contrast with the presence of only two comparable components of similar migration in plasma from control animals. In contrast, no comparable alterations were observed in a comparison of plasma samples from L1210 tumor-bearing DBA mice and the corresponding plasma from animals immune-suppressed with antilymphocytic serum or in control plasma from DBA control plasma from DBA control animals. Analysis of selective binding using iodinated lectins revealed significant binding of I125 Lens culinaris in the more cathodic 75 kd component present in the plasma from control C57 black mice and a decreased Lens culinaris binding in the corresponding plasma components from EL-4 tumor-bearing C57 black animals. An identical assay with the same samples using I125 Ricinus communis did not show significant interaction with any 75 kd protein species, revealing instead lectin binding in components with molecular weights of about 70 and 50 kd. Our results suggest the use of combined two-dimensional electrophoretic separation and relative lectin binding in the analysis of tumor-specific and tumor-associated changes in plasma samples from tumor-bearing individuals.

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