[Isolation, purification and characterization of human proteinase inhibitor, alpha 2-macroglobulin].

A study of the isolation, purification and characterization of human proteinase inhibitor, alpha 2-macroglobulin (alpha 2-M) is presented. The alpha 2-M, with a purity of more than 90% and subunit molecular weight of 185kDa, was isolated by ammonium sulfate fractionated precipitation from human blood plasma and purified by DEAE cellulose DE52 column chromatography. It was found to be the same as the standard counterpart provided by sigma company. This purification procedure of alpha 2-M can be done with low cost, high efficiency and in large scale preparation.