Isolation and partial characterization of a mucin-type glycoprotein from plasma membranes of human melanoma cells |
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Authors: | Junji Umemoto VP Bhavanandan Eugene A Davidson |
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Institution: | Department of Biological Chemistry, and Specialized Cancer Research Center, The Milton S. Hershey Medical Center, The Pennsylvania State University, Hershey, PA 17033 U.S.A. |
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Abstract: | Plasma membranes were isolated from HM7 melanoma cells grown in the presence of 3H]glucosamine and Na235SO4 or 3H]mannose and 14C]glucosamine. The labelled glucoconjugates were solubilized with 0.6 M lithium diiodosalicylate/0.5% Triton X-100. Fractionation of glycoconjugates by repeated chromatography on columns of Sepharose CL-6B and DEAE-Sepharose and by affinity chromatography on WGA-Sepharose yielded three radiochemically homogenous glycoproteins. One of these having an apparent molecular weight of 100 000 was found to contain clusters of (AcNeu)1 or in2 å Gal å GalNAc] linked to the protein. One other glycoprotein contained both and oligosaccharides, and the third contained only carbohydrates. Preliminary results indicate that the 100 000 molecular weight mucin-type glycoprotein is present in significantly reduced quantities in cultured human fetal uveal melanocytes. Further, the bulk of the glycoproteins from the melanocytes were of lower molecular size compared to those from the melanoma cells. |
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Keywords: | Glycoprotein isolation Plasma membrane Mucin (Human melanoma cell) WGA wheat germ agglutinin AcNeu GalNAc(OH) To either of whom correspondence should be addressed |
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