Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

Similarities in amino acid sequences, three-dimensional structures, and the exon-intron patterns of their genes have indicated that c-type lysozymes and alpha-lactalbumins are homologous proteins, i.e., descended by divergent evolution from a common ancestor. Like the alpha-lactalbumins, echidna milk, horse milk, and pigeon eggwhite lysozymes all bind Ca(II). Models of their three-dimensional structures, based on their amino acid sequences and the known crystal structures of domestic hen eggwhite and human lysozymes and baboon and human alpha-lactalbumins, have been built. The several structures have been compared and their relationships discussed.

Type

Journal article

Journal

J Protein Chem

Publication Date

08/1994

Volume

13

Pages

569 - 584

Keywords

Amino Acid Sequence, Animals, Binding Sites, Biological Evolution, Calcium, Columbidae, Echidna, Egg Proteins, Horses, Isoenzymes, Lactalbumin, Milk Proteins, Molecular Sequence Data, Muramidase, Protein Conformation