Studies on immunological properties of enolase from carp muscles (Cyprinus carpio) after chemical modification of some amino-acid residues.
After modification of histidine residues, enolase from carp muscles lost the ability to precipitate with antibodies against native enzyme. This ability remained after nitration of tyrosine residues, but the immunoelectrophoretic pattern--localisation and height of arcs--differed from that of native enolase. Minor changes of this pattern were found in enolase with modified tryptophan residues.
D000596:Amino Acids / Q000276:immunology*; D000818:Animals; D002347:Carps / Q000378:metabolism*; D003530:Cyprinidae / Q000378:metabolism*; D000939:Epitopes / Q000276:immunology; D006639:Histidine / Q000378:metabolism; D007122:Immunoelectrophoresis / Q000379:methods; D007123:Immunoelectrophoresis, Two-Dimensional / Q000379:methods; D009132:Muscles / Q000201:enzymology*; D010751:Phosphopyruvate Hydratase / Q000276:immunology*; D011499:Protein Processing, Post-Translational; D013329:Structure-Activity Relationship; D014364:Tryptophan / Q000378:metabolism; D014443:Tyrosine / Q000378:metabolism
D000596:Amino Acids; D000939:Epitopes; D014443:Tyrosine; D006639:Histidine; D014364:Tryptophan; D010751:Phosphopyruvate Hydratase