The N, O-diacetylmuramidase of chalaropsis species. IV. Tryptic peptides.
Lysozyme Ch was hydrolyzed with trypsin in 2 M urea and the resulting peptides were separated by a combination of gel filtration and ion exchange chromatography. Ten peptides and free lysine were produced by tryptic action. The enzyme has 5 arginine and 4 lysine residues per molecule and one of the peptides arose from a chymotryptic-like cleavage of a tyrosyl-seryl bond near the amino-terminal end of the enzyme. The entire molecule is accounted for by the tryptic peptides, which have been ordered withing the peptides obtained by cyanogen bromide cleavage of the molecule.
D000085:Acetates; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003488:Cyanogen Bromide; D003904:Mitosporic Fungi / Q000201:enzymology*; D009113:Muramidase; D010446:Peptide Fragments / Q000032:analysis; D014357:Trypsin
D000085:Acetates; D000596:Amino Acids; D010446:Peptide Fragments; D009113:Muramidase; D014357:Trypsin; D003488:Cyanogen Bromide