BIOSPECIFIC AFFINITY CHROMATOGRAPHIC PURIFICATION OF OCTOPINE DEHYDROGENASE FROM MOLLUSKS

The development of a biospecific affinity chromatographic method for t he purification of octopine dehydrogenase from molluscs is described. The method utilizes immobilized NAD(+) derivatives in conjunction with soluble specific substrates to promote binding. Using this method, oc topine dehydrogenase has been purified to electrophoretic homogeneity in a single chromatographic step from three different marine invertebr ate sources [the queen scallop, Chlamys opercularis (adductor muscle), the great scallop, Pecten maximus (adductor muscle), and the squid Lo ligo vulgaris (mantle muscle)]. However, the system is not applicable to the purification of octopine dehydrogenase from some other marine i nvertebrate sources investigated (the mussel Mytilus edulis and the to pshell Monodonta lineata). (C) 1997 Academic Press.