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Pigeon egg white lysozyme. Purification, structural and enzymic characterization

J G Gavilanes, G G de Buitrago, A M del Pozo

International Journal of Peptide and Protein Research

|September 1, 1982

Summary

Pigeon egg white lysozyme was purified and characterized, revealing properties similar to chicken lysozyme c. This study details its lytic activity, stability, and molecular features.

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Area of Science:

Biochemistry
Enzymology

Background:

Lysozymes are crucial enzymes with antibacterial properties.
Characterizing avian lysozymes provides insights into enzyme evolution and function.

Purpose of the Study:

To purify and biochemically characterize lysozyme from pigeon egg white.
To classify the pigeon lysozyme based on its properties.

Main Methods:

Ion exchange chromatography and gel filtration for purification.
Enzyme activity assays, pH and ionic strength studies.
Thermal stability, molecular weight, and amino acid composition analysis.

Main Results:

Lysozyme was purified with a 65% yield and specific activity of 15,000 units/mg.

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Lytic activity, thermal stability, molecular weight, and amino acid composition were determined.

The pigeon enzyme was classified as a chicken-type lysozyme (lysozyme c).

Conclusions:

Pigeon egg white lysozyme shares characteristics with chicken lysozyme c.
The purification and characterization provide a foundation for further studies on avian lysozymes.