Carcinoembryonic antigen (CEA) was elevated ( > 2.5 ng/ml) in 81 of 100 patients with gynecologic malignancy and in 17 of 95 patients with benign gynecologic disease. CEA concentration was, in general, related to the extent of disease, and in early stage cancer often returned to normal following complete surgical excision. Tumors were classified morphologically according to cell type, lymphoplasmacytic infiltration, necrosis, vascular invasion, desmoplasia, and degree of differentiation. The only histologic characteristic associated with elevated CEA levels was the presence of vascular invasion. Further investigation is needed to define the structure, function, and metabolism of CEA in patients with gynecologic malignancy.
Under conditions that are optimum for DbetaH, ascorbic acid denatures serum albumin, gamma-globulin, catalase, and DbetaH. With ascrobate plus Cu2+, the proteins are almost completely destroyed. Pyrazole protects DbetaH and albumin, but not catalase. Superoxide dismutase (SOD) is not denatured by ascorbate, with or without Cu2+, and in combination with catalytic amounts of catalase or Fe2+ it stimulates maximum DbetaH activity. In other words, a combination of catalase and SOD, or Fe2+ and SOD, will protect DbetaH. Excessive amounts of catalase and/or other protein, either native or denatured will prevent the effects of superoxide and/or ascrobate, but cannot replace the requirements for catalytic quantities of catalase or Fe2+. The results suggest that the rate of hydroxylation of tyramine may be limited by superoxide, but that the latter per se does not denature DbetaH as does hydrogen peroxide. The in vitro activation of oxygen by DbetaH is a toxic process, involving the production of both hydrogen peroxide and superoxide and possibly other free radicals. In the absence of precise regulation of the production and concentrations of these compounds, the enzyme is denatured.
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