Abstract
Plasminogen activator in spent tissue culture medium from a continuous line of pig kidney cells was purified on a 25 liter scale by a combination of adsorption on hydroxyapatite, ammonium sulfate precipitation, DEAE-and CM-cellulose chromatography, and gel filtration. The final product had a specific activity of 70,000 to 120,000 units/mg and consisted of numerous immunologically similar species of different size and charge. Two major fractions were obtained by gel filtration. The principal fraction included enzymes of molecular weights >45,000. The other fraction included 30,000 and 24,000 dalton forms. The large forms could be degraded to smaller forms. The isolectric points of the different species were in the range pH 6.8 to 7.2. Active site titrations gave 1.4 ± 0.1 × 10 13 units/mole. The enzyme was similar to, but not identical with, human urokinase in specificity, inhibitor sensitivity, and fibrinolytic activity. The two enzymes were immunologically different.
Published Version
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