title: [Modification of histidine residues with diethylpyrocarbonate in aspartate transaminases from pig and chicken heart cytosol].
abstract: One and three histidine residues react with diethylpyrocarbonate (DEP) at pH 6.5 in native aspartate transminases from cffect on the enzyme activity. The rest histidine residues in aspartate transaminases (approximately 6 in the chicken enzyme and 5 in the pig enzyme) are DEP-nonreactive and can be carbetoxylated only after protein denaturation. The presence of substrates does not affect the histidine modification in transaminases.
mesh_terms: D000818:Animals; D001219:Aspartate Aminotransferases / Q000378:metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D002645:Chickens; D003600:Cytosol / Q000201:enzymology; D004047:Diethyl Pyrocarbonate; D005561:Formates; D006639:Histidine; D009206:Myocardium / Q000201:enzymology*; D011489:Protein Denaturation; D013329:Structure-Activity Relationship; D013552:Swine
chemical_list: D005561:Formates; D006639:Histidine; D001219:Aspartate Aminotransferases; D004047:Diethyl Pyrocarbonate
vernacular_title: Modifikatsiia ostatkov gistidina v tsitorlazmaticheskikh aspartat-transaminazakh svin'i i kuritsy pri pomoshchi dietilpirokarbonata