ABSTRACT
This chapter reviews the data on the physical, chemical, and enzymatic properties of cancer procoagulant. Cancer procoagulant enzymatic activity or antigen was found in virtually every kind of malignant tissue examined, suggesting it is a widely distributed oncogenic protein. The purified antibody was coupled to a cyanogen bromide-activated sepharose and an immunoaffinity column to cancer procoagulant was prepared and used for purification of large amounts of cancer procoagulant antigen. With the rapid and relatively simple purification of cancer procoagulant antigen, it became feasible to develop monoclonal antibodies. Cancer procoagulant is neither FVIIa or FIXa, because it has a different molecular weight, amino acid composition and carbohydrate content, and it is a cysteine proteinase in contrast to the serine proteinase characteristics of FVIIa and FIXa. In the first series of experiments we looked for cancer procoagulant activity in a variety of normal and malignant cells and tissue.
