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- W2064012256 abstract "The molecular nature of SGA, the ovarian-carcinoma-associated antigen defined by the MAb OM-1, has been determined. The cell-surface form of the SGA molecule is a glycoprotein with p1 less than 4.2, which on PAGE analysis has an apparent MW of approximately 360 kDa. This was the only OM-1-reactive species found on the cell surface. The apparent MW was unaffected by reducing conditions. The predominant cytoplasmic form of SGA is a non-glycosylated 170-kDa molecule with p1 6.5. Pulse-chase experiments were complicated by the extremely slow rate of SGA synthesis. However, the data indicate that the SGA molecule is synthesized as a 190-kDa protein, cleaved to yield a 170-kDa non-glycosylated intracellular form which is slowly glycosylated to the 360-kDa cell-surface species. Western blotting experiments revealed the presence of the 360-kDa glycosylated molecule in human ovarian cell culture supernatants." @default.
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- W2064012256 date "1986-05-15" @default.
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- W2064012256 title "Biochemical characterization of the monoclonal antibody-defined ovarian carcinoma-associated antigen SGA" @default.
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- W2064012256 doi "https://doi.org/10.1002/ijc.2910370511" @default.
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