Abstract

This paper reports the separation of highly cationic proteins (i.e. pI greater than 9.0) of bovine allantoic fluid and their possible pathogenic properties. Experimentally, polycations and cationic proteins of pI greater than 10 induced intravascular coagulation and hemolysis, as well as precipitation of fibrinogen and proteinuria. Bovine allantoic fluid collected at the time of calving contains from 0.6 to 1.3 g of proteins per liter (11 samples). Ion-exchange chromatography, followed by either chromatofocusing or heparin-sepharose-6 beta binding, and, finally, gel filtration separated several fractions and subfractions. These were examined later using polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, and at least ten constituents were visualized. Two components, Mr 34,000, pI 9.7, and Mr 38,000, pI 9.6-9.0, accounted for 33% of the basic proteins present in allantoic fluid and 0.7% of its total protein content. Electrophoretic mobility was unaltered by beta-mercaptoethanol, and periodic acid-Schiff staining was negative. These proteins were not found in ox plasma. The major basic proteins were bound to red cells and platelets. Cell electrophoretic mobility decreased linearly with the logarithm of protein concentration. At concentrations between 10(-6) and 10(-5) M, red cell clumping was rare; hemolysis and platelet agglutination were not observed.

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