Abstract
A plasma protein which forms a precipitation line with antiserum against urinary trypsin inhibitor was purified by ammonium sulphate fractionation, anti-urinary trypsin inhibitor rabbit IgG antibody coupled sepharose immunoadsorbent column chromatography and polyacrylamide-gel disc electrophoresis. By these procedures, 0.14 mg of purified material was obtained from 20 ml of plasma. It was homogenous as ascertained by sodium dodecyl sulphate polyacrylamide-gel disc electrophoresis and had an apparent molecular weight of 90,000. It was found that this inhibitor was immunologically distinct from inter-α-trypsin inhibitor.