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Isolation of the JMH antigen on a novel phosphatidylinositol-linked human membrane protein

KA Bobolis, JJ Moulds and MJ Telen

Department of Medicine, Duke University Medical Center, Durham, NC 27710.

JMH is a high-frequency human erythrocyte blood group antigen. Previous work has shown that JMH is absent from complement-sensitive erythrocytes of patients with paroxysmal nocturnal hemoglobinuria (PNH); such cells have a broad defect in expression of phosphatidylinositol (PI)-linked proteins. Using both human JMH antisera and a JMH-like murine monoclonal antibody, we have identified a 76-Kd membrane protein present in JMH-positive but not JMH-negative erythrocytes. A similar 76-Kd JMH protein was also identified on a human lymphoid T-cell line, HSB-2. Using PI-specific phospholipase C, a small amount of JMH antigen could be cleaved from intact erythrocytes and immunoprecipitated from the supernate of treated erythrocytes, thus confirming that the protein bearing the JMH antigen is anchored by a PI- linkage to the erythrocyte membrane. This protein was further shown not to be identical to decay accelerating factor (70 Kd), a previously identified PI-anchored protein of somewhat similar molecular weight.

Volume 79, Issue 6, pp. 1574-1581, 03/15/1992
Copyright © 1992 by The American Society of Hematology


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A. Yamada, K. Kubo, T. Takeshita, N. Harashima, K. Kawano, T. Mine, K. Sagawa, K. Sugamura, and K. Itoh
Molecular Cloning of a Glycosylphosphatidylinositol-Anchored Molecule CDw108
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[Abstract] [Full Text] [PDF]



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  Copyright © 1992 by American Society of Hematology         Online ISSN: 1528-0020