Ultra-high Yield Intravenous Immune Globulin Preparation

Abstract

An efficacious large-scale alcohol-free plasma fractionation production process which produces a high-yielding, non-denatured, double viral-inactivated intravenous human immune gamma globulin (IgG) product. The process employs one or more salts from a group of salts comprising sodium citrate, sodium acetate, sodium gluconate, ammonium sulfate, sodium chloride, sodium sulfate and ammonium chloride in two initial fractionation steps, followed by diafiltration to remove those salts employed. A process which employs alcohol via the process of the disclosed inventive method is also disclosed.

Description

[0001]This Application for Patent is a Divisional of U.S. patent application Ser. No. 11 / 358,431, filed Feb. 21, 2006, which is a Continuation-in-Part of U.S. patent application Ser. No. 11 / 232,527, filed Sep. 22, 2005, which is a Continuation-in-Part of U.S. patent application Ser. No. 11 / 217,956, filed Sep. 1, 2005.FIELD OF INVENTION[0002]This invention relates generally to methods for immune serum globulin purification, and, more particularly, to methods for alcohol-free separation of immune globulin from blood plasma or other blood based material. Interestingly, the method of the instant invention also may be employed using alcohol.BACKGROUND AND DESCRIPTION OF RELATED ART[0003]Commonly, contemporary methods for separation of immune globulins (IgG) from blood plasma or other blood based material depend upon early work by Edwin J. Cohn. As found in U.S. Pat. No. 5,177,194 issued Jan. 5, 1993 to Maria E. Samo, et al. (SARNO), “One scheme in widespread use is the well-known Cohn fr...

AI Technical Summary

Benefits of technology

[0016]Also, addition of these salts to protein in solution proves to be not as reactive to removal of water as addition of ethanol by previous methods. A rapid isolation using these salts, removal of the resulting fraction followed by removal of salt from the resulting fraction and a quick restoration of the internal water molecule of the protein has proved superior to ethanol fractionation using currently employed methods.

[0037]It is an object to produce gamma globulin having reduced in-process formation of polymers, aggregates, fragments, enzyme activators and proteolytic enzymes compared with similar preparations produced using traditional alcohol-based methods.

Problems solved by technology

Even so, the use of alcohol precipitants is not without difficulties, as illustrated by Cohn, “Some protein precipitants, such as alcohol, have a tendency to denature many proteins with which they come in contact, the danger of denaturation increasing with concentration of the alcohol and increase in temperature.

Such binding may be a cause of changes in protein configuration resulting in some permanent denaturation of protein molecules which remains after ethanol is removed and water is returned.

However, chromatographic separation of the large-weight, lower-value fractions such as albumin and gamma globulin, on an industrial scale has not been found to be practical.

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