Biospecific affinity chromatographic purification of octopine dehydrogenase from molluscs.
The development of a biospecific affinity chromatographic method for the 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, octopine dehydrogenase has been purified to electrophoretic homogeneity in a single chromatographic step from three different marine invertebrate sources [the queen scallop, Chlamys opercularis (adductor muscle), the great scallop, Pecten maximus (adductor muscle), and the squid Loligo vulgaris (mantle muscle)]. However, the system is not applicable to the purification of octopine dehydrogenase from some other marine invertebrate sources investigated (the mussel Mytilus edulis and the topshell Monodonta lineata).
Mulcahy
P
P
Department of Biochemistry, University College Galway, Ireland.
Griffin
T
T
O'Carra
P
P
D000249:Adenosine Monophosphate / Q000031:analogs & derivatives; D000594:Amino Acid Oxidoreductases / Q000302:isolation & purification*; D000818:Animals; D002846:Chromatography, Affinity / Q000379:methods*; D049832:Decapodiformes / Q000201:enzymology; D008974:Mollusca / Q000201:enzymology*; D009132:Muscles / Q000201:enzymology*; D009243:NAD / Q000031:analogs & derivatives; D013045:Species Specificity
D009243:NAD; D000249:Adenosine Monophosphate; D000594:Amino Acid Oxidoreductases; C021903:D-octopine dehydrogenase