Abstract
The preparation of albumin from human or animal blood serum is described. Serum or plasma is treated with acidified lower alcohols, whereby the globulins are precipitated, leaving the albumin in the supernatant liquid. It is shown that low concentrations of certain very strong acids are sufficient to retain substantially the whole of the albumin in solution. From this acid solution, by neutralization, the albumin is precipitated in a form almost undenatured and free from globulins. With weaker acids, or with acetone as solvent, the resulting albumin is in most cases partially denatured. The conditions governing this separation are discussed and the results compared with recent similar work described in the literature. Some observations on the solubility of other proteins in acidified alcohols are mentioned.