Cohn process

The Cohn process, developed by Edwin J. Cohn, is a series of purification steps with the purpose of extracting albumin from blood plasma. The process is based on the differential solubility of albumin and other plasma proteins based on pH, ethanol concentration, temperature, ionic strength, and protein concentration.[1][2] Albumin has the highest solubility and lowest isoelectric point of all the major plasma proteins. This makes it the final product to be precipitated, or separated from its solution in a solid form. Albumin was an excellent substitute for human plasma in World War Two. When administered to wounded soldiers or other patients with blood loss, it helped expand the volume of blood and led to speedier recovery. Cohn's method was gentle enough that isolated albumin protein retained its biological activity.[3]

  1. ^ Foster, Peter (1994). The Kirk -Othmer Encyclopedia of Chemical Technology, 4th edition, vol 11, 990-1021. pp. 990–1021.
  2. ^ Cohn, E. J.; Strong, L. E.; Hughes, W. L.; Mulford, D. J.; Ashworth, J. N.; Melin, M.; Taylor, H. L. (1946). "Preparation and Properties of Serum and Plasma Proteins. IV. A System for the Separation into Fractions of the Protein and Lipoprotein Components of Biological Tissues and Fluids1a,b,c,d". Journal of the American Chemical Society. 68 (3): 459–475. doi:10.1021/ja01207a034. ISSN 0002-7863. PMID 21015743.
  3. ^ Surgenor, Douglas. Edwin J. Cohn and the Development of Protein Chemistry. Center for Blood Research.