Comparison of affinity membranes and conventional affinity matrices with regard to protein purification

Abstract

Binding capacities for purified malate dehydrogenase from pig heart and malate dehydrogenase from Escherichia coli were determined for different gel matrices and a Cibacron Blue modified membrane. During batch adsorption the membrane has nearly the same capacity as Blue Sepharose. During filtration the effective capacity of the membrane was increased in contrast to Blue Sepharose. With cell homogenates, when used under cross-flow conditions, the membrane displayed better performance than Blue Sepharose.