http://pdbbeta.rcsb.org/pdb/explore.do?structureId=3lzt

Other coordinates can be found via http://us.expasy.org/cgi-bin/view-pdb?src=P00698

Not known

Roy et al. (2003) [1335] describes the simultaneous purification of lysozyme, ovalbumin, and ovomucoid from hen egg white. The crude egg white extract was passed through a cation exchanger (Streamline SP). and the bound lysozyme was eluted with 5% ammonium carbonate, pH 9.0, containing 1 M NaCl after elution of avidin. Lysozyme was further purified 639-fold on dye-linked cellulose beads.

Archer et al. (1990) [1362] reported one of the first successful heterologous expressions of a disulphide linked enzyme with lysozyme in Aspergillus.

The structure of several complexes of lysozyme with specific antibody binding sites have been determined (Cauerhff et al. 2004 [1304]; Li et al. 2003 [1261]; Mohan et al. 2003 [1263]; Holmres et al. 2001 [1264]; Bentley, 1996 [1265]; Smith-Gill, 1996 [1266]) and lysozyme is the best understood example of a folded model protein antigen.

Hashida et al. (2002) [1271] showed that healthy fasted volunteers had serum concentrations of 1700 pg/ml. of lysozyme (as measured by immuno assay) one hour after eating 90 mg. of lysozyme.

So et al. (2001) [1272] show that lysozyme's allergenicity in a mouse model can be increased by engineering to make lysozyme less stable.

Hen egg white lysozyme is 95-96% identical with sequences from the eggs of birds such as quail and turkey. Other known bird lysozymes are at least 78% identical. Sequences from reptiles such as turtle are 68% identical while bovine milk lysozyme is 60% identical. IgE cross-reactivity would be expected between birds but has not been reported with mammalian lysozymes.