The physiological role of the fibrinolytic system in maintaining the fluidity of the blood is now generally accepted [2]. The persistence of intravascular clots may be associated in part with some deficiency of the normal fibrinolytic mechanism. I n view of the frequency of thrombotic episodes the need for an effective, rational fibrinolytic therapy is very great, particularly in dangerous situations where clots form or lodge in the pulmonary, cerebral or coronary vascular systems. There are three fundamental approaches t o thrombolysis. The first is based on the induction of a fibrinolytic state b y adding amounts of fibrinolysin more than sufficient t o overcome the antifibrinolysin. The second approach is based on the ability of a n "activator" t o induce a fibrinolytic state. The third approach is to use a combination of a n activator and the fibrinolysin. A number of materials are being studied as activators to induce a fibrinolytic state: such as, streptokinase [7], urokinase [14], pyrogens [8], and chemicals [27].Our report deals with a study involving the preparation for clinical evaluation of human fibrinolysin with and without the activator, urokinase. The source of our profibrinolysin was the Fraction I11 paste usually discarded in the preparation of gamma globulin from outdated blood [S, 131. The source of the activator, urokinase, was stable a t neutral pH a t 25" C. These solutions are readily prepared in sterile condition for clinical use. All protein components have been subjected to a heat treatment period of 10 hours a t 60" C. during their purification. MaterialsBlood protein source. Human plasma Fraction I11 paste was kindly provided by the Blood Program of the American National Red Cross. This fraction was prepared b y Method 6 of Cohn, et al. [5] and Method 9 of Oncley, et al. [13] by E. R. Squibb & Sons, New Brunswick, New Jersey. Glycerol. Shell Chemical Corporation, 99.5 % U.S.P. synthetic glycerol. Phosphate-saline bufler. p H 7.4, 0.1 M sodium phosphate -0.9% NaCl buffer.Streptokinase. Lederle Varidase(R) was dissolved in phosphatesaline buffer a t 3,000 units per milliliter and stored a t 0-2" C.Casein solution. Devitaminized and high nitrogen caseins were kindly supplied by the Sheffield Company+. Stock solutions of 6% (w/v) casein were prepared by dissolving the material in 0.1 M phosphate-saline buffer and adjusting the p H to 7.4 with 1 N NaOH. The solution was heated in a boiling water bath for 15-30 minutes t o destroy any proteolytic activity present. The final solution was filtered, adjusted to p H 7.40 and stored in 50 ml. volumes in the frozen state (-30" C.).

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Hepatitis B Antigen (HB Ag) has been found in human blood capable of transmitting viral hepatitis. HB Ag and anti‐HB Ag were therefore sought in the cold ethanol fractions of plasma from HB Ag+ patients collected into three different anticoagulant solutions, in fractions from individuals with anti‐complementary plasma containing anti‐HB Ag, and in fractions from large pools of ACD plasma from normal blood donors. HB Ag was present in all Cohn fractions except Fraction II (immune serum globulin, ISG) when prepared from HB Ag+ plasma regardless of the anticoagulant used. Five of eleven production lots of ISG and one of six NSA preparations contained measurable quantities of anti‐HB Ag, but none contained HB Ag. Antibody to HB Ag was detected in Cohn Fractions I, II, III and, to a lesser extent, in V after the cold ethanol process when prepared from plasma from HB Ag+ hepatitis patients. Despite the simultaneous presence of HB Ag and anti‐HB Ag, these plasmas were not anticomplementary. HB Ag was not found in fractions of plasma from individuals with anti‐HB Ag whose sera were anticomplementary. The radioimmunoassay technics for detecting HB Ag in Fraction II and ISG gave false positive reactions. Despite the improved sensitivity of these technics, they cannot be relied upon to give meaningful analyses for HB Ag in ISG preparations. In testing ISG for antibody to HB Ag, however, the hemagglutination and radioimmunoprecipitation tests appeared to give reliable results.

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