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TÜBİTAK

Journal

2001

Purification

Articles 1 - 2 of 2

Full-Text Articles in Physical Sciences and Mathematics

A Comparative Study On The Recovery Of Ecori Endonuclease From Two Different Genetically Modified Strains Of Escherichia Coli, Candan Tamerler, Zeynep İlsen Önsan, Betül Kirdar Jan 2001

A Comparative Study On The Recovery Of Ecori Endonuclease From Two Different Genetically Modified Strains Of Escherichia Coli, Candan Tamerler, Zeynep İlsen Önsan, Betül Kirdar

Turkish Journal of Chemistry

A laboratory scale procedure developed for the purification of EcoRI restriction endonuclease was applied to two different Escherichia coli} strains, E. coli 294 and E. coli M5248, which are genetically modified to overproduce the enzyme. The purification method consisted of three successive chromatographic steps including phosphocellulose and hydroxyapatite columns and further fractionation in a second phosphocellulose column. It was shown that the second phosphocellulose separation can be omitted in the case of E. coli 294. Quality control tests indicated enzyme preparations free of contaminants and endo- or exo-nucleases. The yields obtained at the final stage of the purification were 1.3x10^{5} …


Purification And Partial Characterisation Of Superoxide Dismutase From Chicken Erythrocytes, Tüli̇n Aydemi̇r, Leman Tarhan Jan 2001

Purification And Partial Characterisation Of Superoxide Dismutase From Chicken Erythrocytes, Tüli̇n Aydemi̇r, Leman Tarhan

Turkish Journal of Chemistry

Superoxide dismutase (SOD), which plays a very important role in protecting organisms from oxygen toxicity, was purified from chicken erythrocyte and partially characterised. Erythrocyte membranes were disintegrated via freeze-thaw methods in the presence of Triton X-100. Following ethanol precipitation, SOD-containing solution was applied to DEAE-cellulose and then Sephadex G-100 gel columns. Chicken erythrocyte SOD was purified 508-fold with a specific activity of 8,480 units per mg. The molecular weight was estimated to be 30.6 kDa \pm 0.4 by gel filtration. The enzyme was composed of two subunits of equal size and contained one atom of copper and one atom of …