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Heaney-Kieras J, Bystryn JC: Identification and purification of 115- and 125-kilodalton cell surface human melanoma-associated antigens. J Natl Cancer Inst. 1986 Sep;77(3):643-8.
Surface macromolecules shed into culture medium by radioiodinated human melanoma cells were fractionated on Sepharose 6B and by sequential lectin-affinity chromatography. Radioactivity associated with melanoma-associated antigens (MAAs) was assayed by indirect immunoprecipitation with anti-melanoma serum. Two MAAs were separated and highly purified. Both antigens were single-chain glycoproteins expressed on many, but not all, melanoma cells but undetectable on normal melanocytes and a variety of unrelated normal, fetal, and malignant cells. One MAA, with a molecular mass of approximately 115 kd, eluted on Sepharose 6B in a lower molecular mass peak and had a high affinity for ricin lectin. The carbohydrate side chain of this antigen contained D-galactose. The other MAA, with a molecular mass of approximately 125 kd, eluted on Sepharose 6B in a peak of higher molecular mass and had a high affinity for wheat germ lectin. The carbohydrate side chain of this antigen contained sialic acid. Both antigens were highly purified. By sodium dodecyl sulfate-poly-acrylamide gel electrophoresis analysis, no contaminating proteins were present in the purified 115-kd MAA fraction, and only a single minor contaminant was present in the fraction containing the purified 125-kd MAA. These two antigens differed in their biochemical or immunological properties from other MAAs of similar size that have been previously described. |
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