title: Relationship between composition and stability of bovine milk lysozyme.
abstract: The amino acid analysis, peptide mapping, and heat stability of bovine milk lysozyme are presented. The bovine milk lysozyme molecule contains approximately 154 amino acids and is strikingly different in amino acid content from human milk lysozyme and egg white lysozyme. Tryptic hydrolysis yielded 26 peptides, all of which are unique from tryptic peptides of human milk lysozyme and egg white lysozyme. In addition, bovine milk lysozyme was more heat stable than human milk lysozyme at pH 4.0 but more labile at pH 7.0 and 9.0. Possible explanations for the differences in heat stability are discussed.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D002942:Circular Dichroism; D004355:Drug Stability; D004529:Egg White; D005260:Female; D006358:Hot Temperature; D006801:Humans; D008892:Milk / Q000201:enzymology*; D008895:Milk, Human / Q000201:enzymology; D009113:Muramidase; D010446:Peptide Fragments; D013045:Species Specificity; D014357:Trypsin
chemical_list: D000596:Amino Acids; D010446:Peptide Fragments; D009113:Muramidase; D014357:Trypsin