Abstract
A surface-localizing heterologous antibody against the mouse Ehrlich ascites carcinoma could be bound to chlorambucil without causing the loss of alkylating activity of chlorambucil or interfering with the reactivity of the antibody with tumor cells. Chlorambucil, when bound to the antibody, was a much more effective tumor inhibitor, both in vitro and in vivo, than chlorambucil or the antibody alone.
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