Partial purification and some properties of aspartate aminotransferase from the mantle tissue of Mytilus galloprovincialis Lam

Authors : Özlem DÖNMEZ YURTPINAR, Tuğba YILMAZ ÖZDEN, Ayşe CAN

Pages : 1-10

View : 41 | Download : 10

Publication Date : 2015-01-29

Article Type : Conference Paper

Abstract :Aspartate aminotransferase insert ignore into journalissuearticles values(E.C.2.6.1.1; AST);, is a pyridoxal phosphate dependent enzyme that occurs in virtually all organisms and plays a key role in intermediary nitrogen metabolism. Although AST was purified from a variety of plant and animal sources, it has not been purified previously from mantle tissue of Mytilus galloprovincialis Lam. In the present study we have partially purified AST from the mantle tissue of M. galloprovincialis and investigated some kinetic properties of the enzyme. The partially purified enzyme showed three protein and a single activity band in polyacrylamide gel electrophoresis. It was found that the enzyme exhibited maximum activity at 15ºC and 35ºC and that the activity was decreased at 40ºC and totally lost at 55ºC. AST activity was maximum at pH 7.4 in Tris-HCl buffer. Km values of AST for aspartate and 2-oxoglutarate were 1.64 mM and 2.2x10-2 mM, respectively, and Vmax values for the same substrates were 0.12 U/mL and 0.168 U/mL, respectively
Keywords : aspartate aminotransferase, Mytilus galloprovincialis Lam, mussel, enzyme purification

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