Purification and characterization of glycogen phosphorylase b from the breast muscle of fruit bat, <i>Eidolon helvum</i> Kerr.

• DOI: 10.4314/ijbcs.v1i2.39679
• Publication Date: 2011-11-26T16:02:28Z
• Authors: O O Odekanyin; F K Agboola; I O Adewale; A Afolayan
• Keywords: Sephadex; Sodium fluoride

The kinetic and physicochemical properties of glycogen phosphorylase b from the breast muscle fruit bat, Eidolon helvum Kerr were investigated in order to obtain some information about possible physiological role enzyme meeting energy requirements bat either at initiation or during flight. Glycogen was purified apparent homogeneity with specific activity approximately 37 units/mg protein a yield 4 %. completely dependent on AMP for activity; hence it designated b. native subunit molecular weights as determined by gel filtration Sephadex G-200 SDS-polyacrylamide electrophoresis 187,000 &#61617; 12,600 Da 90,500 1,200 respectively, thus implying that is dimeric protein. Michealis-Menten constants, Km, glucose-1-phosphate 0.06 mg/ml 6.94 mM while Km 0.08 mM. turnover number, kcat, 65.56 s-1. Although sodium fluoride (NaF) sulphate (Na2SO4) their own activated enzyme, observed presence AMP, only caused activation low concentration. optimum pH 6.4. In conclusion, overall results this study showed physically catalytically similar other mammalian sources.International Journal Biological & Chemical Sciences Vol. 1 (2) 2007: pp. 99-107