Abstract: Immunoassays for complement components, complement activation products or, preferably both, can be used to determine an acceptable level of anticomplement activity (AC) in plasma derived biologically active products intended for infusion into a mammal. In one application an ELISA for complement components (CC) such as C1q, C1r or C1s can be used to determine AC in an IgM-enriched immune serum globulin (ISG). In another application, an immunoassay for complement activation products (CAP) is used for a similar determination. In yet a preferred third application, assays for both a CC (such as measuring a decreasing amount of C1r) and a CAP (such as measuring an increasing amount of C4a) are used to assess the relative AC (and safety) of a biologically active, therapeutic preparation.

Abstract: Mild heat-treatment of IgM antibody concentrates diminishes the potential to induce non-specific complement activation without significant loss of normal immunologic effector functions. These IgM immunoglobulin concentrates retain specific antigen binding properties and activate complement when bound to antigen. Preferred product includes at least 20% by weight IgM in an IgM/IgG antibody mixture. Heating is done at a temperature within the range of about 40.degree. C. to 62.degree. C., preferably about 45.degree. to 55.degree. C., in a solution having an acid pH (preferably 4.0 to 5.0) for at least about 10 minutes.

Abstract: Human .alpha..sub.1 -antichymotrypsin (ACT) can be purified from solutions containing human .alpha..sub.1 -proteinase inhibitor (PI) and antithrombin III (AT-III) using chromatography adsorption steps at carefully controlled pH and conductivity. The separated ACT retains in vitro inhibitory capacity and has potential therapeutic use.

Abstract: Mild heat-treatment of IgM antibody concentrates diminishes the potential to induce non-specific complement activation without significant loss of normal immunologic effector functions. These IgM immunoglobulin concentrates retain specific antigen binding properties and activate complement when bound to antigen. Preferred product includes at least 20% by weight IgM in an IgM/IgG antibody mixture. Heating is done at a temperature within the range of about 40.degree. C. to 62.degree. C., preferably about 45.degree. to 55.degree. C., in a solution having an acid pH (preferably 4.0 to 5.0) for at least about 10 minutes.

Abstract: Mild heat-treatment of IgM antibody concentrates diminishes the potential to induce non-specific complement activation without significant loss of normal immunologic effector functions. These IgM immunoglobulin concentrates retain specific antigen binding properties and activate complement specific antigen binding properties and activate complement when bound to antigen. Preferred product includes at least 20% by weight IgM in an IgM/IgG antibody mixture. Heating is done at a temperature within the range of about 40.degree. C. to 62 .degree. C., preferably about 45.degree. to 55.degree. C., in a solution having an acid pH (preferably 4.0 to 5.0) for at least about 10 minutes.

Abstract: A method of purifying a recombinant protein from a solution, such as tissue culture fluid, containing gylcoproteins. The affinity of lectins for specific glycoproteins is assessed and used to select a particular lectin specific for the contaminating glycoprotein(s). A sugar buffer such as alpha methyl mannoside prevents binding of the recombinant protein. The preferred lectin is lentil lectin, for use in separating recombinant Factor VIII from tissue culture fluid contaminated with rodent protein from the cell line used to produce the recombinant Factor VIII.

Abstract: There is disclosed an immunizing composition comprising a non-toxic polysaccharide isolated from gram-negative bacteria, especially from Pseudomonas aeruginosa, covalently coupled to a non-toxic protein from the gram-positive bacterium Micrococcus luteus by means of a 4-12 carbon moiety. To prepare the above immunizing agent, the lipid A portion of lipopolysaccharide from a gram-negative bacterium is separated to give a non-toxic polysaccharide. Reactive aldehyde groups are generated on the non-toxic polysaccharide by selective oxidation. The non-toxic polysaccharide is then covalently coupled to a non-toxic protein isolated from said gram-positive bacterium, Micrococcus luteus, by means of a polyfunctional compound having 4-12 carbon atoms and having at least two functional groups which are reactive to the aldehyde groups on the non-toxic polysaccharide and to the carboxylic groups on the non-toxic protein.

Abstract: An immunizing composition is disclosed and comprises a detoxified polysaccharide from a gram-negative bacterium covalently coupled to a detoxified protein from said gram-negative bacterium by means of a 4-12 carbon moiety. To prepare the above immunizing agent, the lipid A portion of lipopolysaccharide from a gram-negative bacterium is separated to give a detoxified polysaccharide. Reactive aldehyde groups are generated on the detoxified polysaccharide by selective oxidation. The detoxified polysaccharide is then covalently coupled to a detoxified protein from said gram-negative bacterium by means of a 4-12 carbon moiety having functionalities reactive to the aldehyde groups on the detoxified polysaccharide and to the carboxylic groups on the detoxified protein.