Abstract
Multiple forms of lysozyme found in the rat liver were isolated and characterized from cellular organelles.
Isolation of the enzymes was achieved by Sephadex gel filtration and chromatography on CM cellulose-column. The purity of the preparations was examined by electrophoresis on polyacrylamide gel. The nuclear lysozyme moved as a single band indicating homogeneity, whereas other subcellular lysozymes appeared heterogeneous due to presence of more than one band, thus showing partial purity. Although the subcellular lysozymes were similar with respect to enzymatic properties, pH, buffer molarity optima and electrophoretic mobility, differences were observed in elution patterns, responses to nuclear inhibitor and heat sensitivity. Nuclear lysozyme was distinctly different by these criteria as compared to other subcellular lysozymes.
