Fresh frozen plasma (FFP) is prepared in blood banks world-wide as a by- product of red blood cell concentrate preparation. Appropriate clinical use is for coagulation factor disorders where appropriate concentrates are unavailable and when multiple coagulation factor deficits occur such as in surgery. Viral safety depends on donor selection and screening; thus, there continues to be a small but defined risk of viral transmission comparable with that exhibited by whole blood. We have prepared a virus sterilized FFP (S/D-FFP) by treatment of FFP with 1% tri(n-butyl)phosphate (TNBP) and 1% Triton X-100 at 30 degrees C for 4 hours. Added reagents are removed by extraction with soybean oil and chromatography on insolubilized C18 resin. Treatment results in the rapid and complete inactivation of greater than or equal to 10(7.5) infectious doses (ID50) of vesicular stomatitis virus (VSV) and greater than or equal to 10(6.9) ID50 of sindbis virus (used as marker viruses), greater than or equal to 10(6.2) ID50 of human immunodeficiency virus (HIV), greater than or equal to 10(6) chimp infectious doses (CID50) of hepatitis B virus (HBV), and greater than or equal to 10(5) CID50 of hepatitis C virus (HCV). Immunization of rabbits with S/D-FFP and subsequent adsorption of elicited antibodies with untreated FFP confirmed the absence of neoimmungen formation. Coagulation factor content was comparable with that found in FFP. Based on these laboratory and animal studies, together with the extensive history of the successful use of S/D-treated coagulation factor concentrates, we conclude that replacement of FFP with S/D-FFP, prepared in a manufacturing facility, will result in improved virus safety and product uniformity with no loss of efficacy.

Clonal cell strains have been isolated from normal human liver. These cells, while resembling fibroblasts morphologically, function as hepatocytes, as shown by their ability to synthesize and secrete an antigen identical to human serum albumin. Human diploid and aneuploid cell lines from nonliver sources do not exhibit this property. The spectrum of serum proteins synthesized varied from clone to clone and cell line to cell line.

Hepatitis B antigen-associated particles, isolated from sera of antigen carriers, were submitted to affinity chromatography on columns of insolubilized antibodies to normal human plasma. The (7) suggest the presence of DNA in the core of the 42-nm particles. The molecular masses of the polypeptides identified in HBAg, which has a particle weight of approximately 7 X 10-18 g (8), add up to 320,000-490,000 daltons (9, 10), corresponding to 2550 to 3935 amino acids as calculated from the amino-acid composition (8). The lower and upper numbers correspond to the d and y subtypes of HBAg, respectively. Thus the total length of cistrons coding for these polypeptides should correspond to 7,650 to 11,805 nucleotides. The (500 and 0.5 mg/ml, respectively, 25,000, 30 min at 370) and diethylether + Tween 80 (500 and 0.5 mg/ml, respec-

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