Abstract
Lysozyme from pigeon egg white has been purified by ion exchange chromatography and gel filtration. The overall yield of the purification procedure is 65%. The specific activity of the enzyme is 15 000 units/mg. The influence of pH and ionic strength on the lytic activity of the protein, as well as its thermal stability, have been studied. The molecular weight, secondary structure estimation, amino acid composition, NH2- and COOH-terminal sequence of the protein are also reported. The pigeon enzyme has been classified as a chicken type lysozyme (lysozyme c) according to the obtained results.
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