Open AccessDifferences between the Chemical Structures of Duck and Hen Egg‐white Lysozymes
Author(s) -
Jollès J.,
Hermann J.,
Niemann B.,
Jollès P.
Publication year - 1967
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1967.tb00079.x
Subject(s) - lysozyme , egg white , histidine , tyrosine , phenylalanine , white (mutation) , muramidase , chemistry , leucine , biology , biochemistry , amino acid , gene
Histidine‐free duck egg‐white lysozyme III and hen egg‐white lysozyme have similar but not identical structures. some structural differences are reported. The N‐ and C‐terminal sequences are different. The unique histidine and two phenylalanine residues of hen lysozyme are replaced by a leucine and two tyrosine residues, respectively. The more basic character of duck lysozyme III is due to additional arginine residues. Duck egg‐white lysozymes II and III have not entirely identical chemical structures.