Abstract

  Background and Objectives

  Human plasma is a valuable and unique material containing vital proteins such as albumin, immunoglobulin, and coagulation factors which have pharmaceutical applications. The most current process for purification of immunoglobulin is the Cohn fractionation procedure using ethanol. The basic material for production of immunoglobulin in this procedure is fraction II. In the present study, Cohn fractionation was modified appropriately in order to achieve fraction II with a quality suitable for production of intravenous immunoglobulin.

  Materials and Methods

  Various plasma proteins were precipitated using varying concentrations of ethanol under controlled physiochemical conditions such as temperature , pH and ionic strength. The fractionation products as well as the resulting fraction II were tested and analyzed.

  Results

  The results demonstrate that the modified procedure used can result in a pure fraction II with high yield . The procedure was also suitable for all other plasma proteins. The purified fraction II contained acceptable PKA levels according to specifications of pharmacopoeia. The protein structure was also within normal limits. The repeatability of the modified procedure reported was acceptable.

  Conclusions

  The fraction II obtained in the modified Cohn procedure was a suitable intermediate product to be used in production of intravenous immunoglobulin . The PKA levels as well as the protein aggregation were minimal , and the quality of fraction II was standard . The results showed that the present modified Cohn procedure can be easily scaled up to industrial and semi-industrial levels. The resulting fraction II can be used as an intermediate in production of IVIg.

  Key words: Intravenous immunoglobulin, Cohn fraction, Molecular conformation