THE AMINO-ACID SEQUENCE OF EQUINE MILK LYSOZYME
- 1 January 1985
- journal article
- research article
- Vol. 10 (1) , 23-31
Abstract
The amino acid sequence of equine milk lysozyme was elucidated. The determination of the sequence of the N-terminal region of the whole protein, cyanogen bromide fragments, tryptic and chymotryptic peptides and fragments produced by chemical cleavage after Try residues were involved. The protein consists of a single chain of 129 amino acid residues and has a MW of 14647. While equine milk lysozyme has the essential features of a c(chick)-type lysozyme, there is only 51% sequence homology with human milk lysozyme and 50% with domestic hen egg white lysozyme. Some of the implications of the large number of differences are discussed.This publication has 6 references indexed in Scilit:
- X-ray studies of water in crystals of lysozymeJournal of Molecular Biology, 1983
- Chemical and Immunological Properties and Amino Acid Sequences of Three Lysozymes from Peking-Duck Egg WhiteThe Journal of Biochemistry, 1982
- Refinement of human lysozyme at 1.5 Å resolution analysis of non-bonded and hydrogen-bond interactionsJournal of Molecular Biology, 1981
- Equine whey proteinsComparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1981
- Lysozymes. III. Amino acid sequence of pheasant lysozyme. Evolutionary change affecting processing of prelysozymeBiochemistry, 1979
- Primary structure of rat lysozymeBiochemistry, 1977