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Isolation and purification of bio polymers by affinity chromatography part 2 purification of smooth muscle glycogen phosphorylase b ec 2.4.1.1 using biospecific affinity chromatography on glycogen sepharose


Isolation and purification of bio polymers by affinity chromatography part 2 purification of smooth muscle glycogen phosphorylase b ec 2.4.1.1 using biospecific affinity chromatography on glycogen sepharose



Bioorganicheskaya Khimiya 5(1): 100-104



ISSN/ISBN: 0360-4497

A new method for purification of glycogen phosphorylase b (EC 2.4.1.1) from cow uterus was developed. The procedure included extraction by NaF-EDTA solution, (HN4)2SO4 fractionation, preparation of a glycogen-enzyme complex and hydrophobic chromatography on aminohexyl-Sepharose. Affinity chromatography on glycogen-hydrazidosuccinyl-Sepharose enabled the isolation of the enzyme in electrophoretically homogeneous state. The elution of homogeneous phosphorylase b in the presence of AMP and Pi was accompanied by phosphorolysis of the immobilized glycogen. The enzyme was purified about 2500-fold in 12% overall yield.

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Isolation and purification of bio polymers by affinity chromatography 2. purification of smooth muscle glycogen phosphorylase b ec 2.4.1.1 by affinity chromatography on glycogen sepharose. Soviet Journal of Bioorganic Chemistry 5(1): 77-81, 1979

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