Abstract
Twenty Mabs of human or murine origin were studied. Serological characterization was achieved by the gel technique with common, rare, and enzyme-modified RBCs. Three clones bound to cell surface proteins on immunoblots: 1 anti-Lub and 2 Mabs raised to a purified Kell glycoprotein. Four anti-K Mabs precipitated the expected 93kD protein and a dimeric form under non-reducing conditions.
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