Rapid purification of rat liver lactate dehydrogenase ec 1.1.1.27 by dye ligand affinity chromatography

Chang W M.; Lin J K.; Chang C C.; Hsiung K P.

Proceedings of the National Science Council Republic of China Part A Applied Sciences 7(1): 27-31

1983


Accession: 006259810

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Abstract
Dye-ligand chromatography was examined as a method for the purification of lactate dehydrogenase (LDH) from rat liver. Eleven dye-Sepharose gels were assessed for their ability to bind the rat liver LDH. Among 11 Procion dyes used for ligand formation, Procion Blue MX-3G was the most effective in enabling the column to adsorb and desorb rat liver LDH. The enzyme was purified employing Procion Blue MX-3G-Sepharose-4B affinity chromatography to 615-fold with 90% of the total activity recovered. The purified enzyme exhibited 4 enzymatically active protein bands when electrophoresized on polyacrylamide gels. Procion Blue MX-3G irreversibly inactivates rat liver LDH in a time-dependent fashion. The result was interpreted in terms of the ability of LDH to bind Procion dyes.