Structure of the pigeon lysozyme and its relationship with other type c lysozymes.
1. The secondary structure of the pigeon egg-white lysozyme shows important differences when compared to other type c lysozymes. These differences are mainly located at the region comprising residues 77-84. This segment contains one alpha-helix in the lysozymes c studied by means of an X-ray analysis, while the residues at such positions in pigeon lysozyme would form two beta-bends. 2. Analysis of the tertiary structure of the pigeon lysozyme by means of hydropathy profiles reveals that the above segment seems to be more hydrophilic in the pigeon enzyme than in other type c lysozymes. 3. Though a certain similarity to the calcium-binding loop of alpha-lactalbumins is detected in pigeon lysozyme, the circular dichroism spectra of the protein at neutral pH do not change in the presence of Ca2+ ions. 4. The presented structural analysis is discussed in terms of function-structure and antigenicity relationships between the type c lysozymes.
Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad Complutense, Madrid, Spain.
R
R
Rodríguez
L
L
Menéndez-Arias
G
G
Gonzalez de Buitrago
J G
JG
Gavilanes
D000818:Animals; D002118:Calcium / Q000378:metabolism; D002417:Cattle; D002645:Chickens; D010856:Columbidae; D004529:Egg White; D006736:Horses; D006801:Humans; D007527:Isoenzymes; D009113:Muramidase / Q000378:metabolism; D011487:Protein Conformation; D013045:Species Specificity
D007527:Isoenzymes; D009113:Muramidase; D002118:Calcium