title: [Chemical modification of epsilon-NH2 groups of lysine residues in horseradish peroxidase. Accessibility of these groups to different modifying agents].
abstract: Modification of epsilon-NH2 groups of lysine residues in horseradish peroxidase by acetic, propionic, butyric, valeric and succinic anhydrides and trinitrobenzenesulfonic acid (TNBS) is carried out. All the anhydrides modify at 0 degrees C four epsilon-NH2 lysine groups, and TNBS--three groups. TNBS modifies all 6 peroxidase epsilon-NH2 groups at 40 degrees C. Possible spacing of lysine epsilon-NH2 groups in the enzyme molecule is discussed.
mesh_terms: D000812:Anhydrides; D006735:Horseradish Peroxidase; D008239:Lysine; D010544:Peroxidases; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D014302:Trinitrobenzenesulfonic Acid
chemical_list: D000812:Anhydrides; D014302:Trinitrobenzenesulfonic Acid; D006735:Horseradish Peroxidase; D010544:Peroxidases; D008239:Lysine
vernacular_title: Khimicheskaia modifikatsiia epsil'-NH2-grupp ostatkov lizina v peroksidaze iz khrena. Dostupnost' etikh grupp razlichnym modifitsiruiushchim agentam.