Effect of modification on physico-chemical and biological properties of haptoglobin. Acetylation, iodination and nitration.
Human haptoglobin (Hp) type 2-1 was modified with N-acetylimidazole, iodine or tetranitromethane (TNM), and the ability of the obtained derivatives to form with haemoglobin (Hb) complexes with peroxidase activity, was estimated. At low reagent to protein molar ratios, 11 tyrosine residues were nitrated, 12 acetylated and 13 iodinated. The biological activity of NO2-Hp and I-Hp amounted to 40% of the activity of native Hp whereas the activity of Ac-Hp only to 16%. The derivatives modified at high ratios of N-acetylimidazole or iodine lost the ability to bind with Hb. Deacylation. of tyrosines and partial liberation of acetylated xi-amino groups resulted in partial recovery of the activity. As demonstrated by polyacrylamide-gel electrophoresis, the modification of Hp with high excess of TNM or iodine induced polymer formation
D000107:Acetylation; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D006242:Haptoglobins / Q000032:analysis; D006454:Hemoglobins / Q000378:metabolism; D007093:Imidazoles; D007455:Iodine; D010544:Peroxidases / Q000032:analysis; D011108:Polymers; D011485:Protein Binding; D013438:Sulfhydryl Compounds; D013774:Tetranitromethane; D014443:Tyrosine / Q000378:metabolism
D006242:Haptoglobins; D006454:Hemoglobins; D007093:Imidazoles; D011108:Polymers; D013438:Sulfhydryl Compounds; D014443:Tyrosine; D007455:Iodine; D010544:Peroxidases; D013774:Tetranitromethane