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. Author manuscript; available in PMC: 2011 Feb 1.
Published in final edited form as: Comp Biochem Physiol B Biochem Mol Biol. 2010 Feb;155(2):201–209. doi: 10.1016/j.cbpb.2009.11.012

Figure 2.

Figure 2

Purification of lyoszyme c-1 from conditioned medium of 4a3B cells. A. Ion-exchange chromatography of the crude cell culture medium. B. Gel filtration chromatography of peak fractions from A. on Sephadex G-75. C. Silver stained gel from ion-exchange peak and G-75 fractions; Lane IE- ion exchange peak, lanes marked 19-25 are the respective fractions from B. Fraction 22-24 were used for characterization of activity under varied conditions. Lysozyme band is seen at an apparent molecular mass of 14 kDa marked by an arrow.