[Biospecific chromatography of acid proteinases. The role of ionic and hydrophobic interactions].
Pepsin chromatography was studied on peptide ligand sorbents, differing in the length of the polypeptide chains, ionogenic groups and the nature of hydrophobic side groups. Pepsin sorption was found to be dependent of a specific interaction of the substrate analogs with the enzyme and ionic interactions with the matrix and ionogenic groups of the ligand. Non-specific hydrophobic interactions of the enzyme and the ligand have little effect on the sorption. Efficient methods for the isolation of pepsin and separation of the mixture of bovine chymosin and pepsin are described.
D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity; D012085:Chymosin / Q000302:isolation & purification*; D008024:Ligands; D010434:Pepsin A / Q000302:isolation & purification*; D010455:Peptides
D008024:Ligands; D010455:Peptides; D010434:Pepsin A; D012085:Chymosin
Biospetsificheskaia khromatografiia kislykh proteinaz. Vklad ionnogo obmena i gidrofobnykh vzaimodeĭstviĭ