Premium
Exhaustive Proteolysis of Derivatives of Lysozyme
Author(s) -
Sokolovsky M.,
Neumann Hava
Publication year - 1971
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.197100035
Subject(s) - chemistry , lysozyme , proteolysis , pepsin , peptide , peptide bond , threonine , amino acid , serine , alanine , side chain , sequence (biology) , peptide sequence , chromatography , biochemistry , stereochemistry , enzyme , organic chemistry , gene , polymer
The specificity of pepsin action towards a protein substrate, 8‐carboxymethyllysozyme, was investigated. The complex mixture of peptides obtained after 16hr of digestion was fractionated by high voltage paper electrophoresis. The peptide fragments were identified by a computer program and were fitted along the lysozyme sequence. The peptide bonds attacked were generally those that originate from at least one hydrophobic amino acid side chain, though some bonds involving alanine, threonine, and serine, were also found to be split.