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J. Biol. Chem., Vol. 263, Issue 36, 19510-19512, Dec, 1988

Monoclonal antibody against an epitope on the cytoplasmic aspect of the plasma membrane calcium pump

AK Grover
Department of Biomedical Sciences, McMaster University, Faculty of Health Sciences, Hamilton, Ontario, Canada.

Monoclonal antibody PM4A2B was prepared by immunizing mice with calmodulin affinity purified Ca2+-Mg2+-adenosine triphosphatase from rabbit erythrocytes and screening the clones with a plasma membrane- enriched fraction (F1) from rabbit stomach smooth muscle. On Western blots, PM4A2B reacted with F1 and with ghosts, right-side-out vesicles, and inside-out vesicles prepared from erythrocytes giving one major band at 130 kDa and minor lower molecular weight bands whose intensity increased on freezing and thawing the membranes. On enzyme-linked immunosorbent assay, PM4A2B reacted with inside-out vesicles, but not with the right-side-out vesicles or ghosts prepared from erythrocytes. It activated the ATP-dependent Ca2+ uptake by F1 and by the inside-out vesicles prepared from the erythrocytes. PM4A2B should be useful in determining membrane sidedness as well as in investigating the mechanism of the sarcolemmal Ca2+ pump.
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