Belostotskiĭ V M, Andreeva A P
Biokhimiia. 1979 Feb;44(2):240-4.
The effects of modification of heme carboxylic groups by omega-aminoenantic acid and L-phenylalamine on the peroxidase activity of hemoglobin were studied. For this purpose the peroxidase activities of the original compounds--hemin, hemin-aminoenantic acid, hemin-phenylalanine and hemoglobins prepared from the hemin and globin compounds--hemoglobin, aminoenantyl-hemoglobin and phenylalanine hemoglobin--were determined. The dependence of the peroxidase activity of these compounds on their concentrations and pH was analyzed. It was shown that 40--50% modification of the heme carboxylic groups by amino acids decreases the peroxidase activity of the modified hemins and that of modified hemoglobins reconstructed from these hemins and globin. A decrease of the catalytic activity of the hemoglobin derivatives is due to a lower peroxidase activity (as compared to hemin) of the modified hemins. It is thus concluded that the amino acid modification of the carboxylic groups of heme does not affect the heme-protein interactions in the hemoglobin molecule.
研究了ω-氨基对映酸和L-苯丙氨酸对血红素羧基的修饰对血红蛋白过氧化物酶活性的影响。为此，测定了原始化合物——血红素、血红素-氨基对映酸、血红素-苯丙氨酸以及由血红素和珠蛋白化合物制备的血红蛋白——血红蛋白、氨基对映基-血红蛋白和苯丙氨酸血红蛋白的过氧化物酶活性。分析了这些化合物的过氧化物酶活性对其浓度和pH值的依赖性。结果表明，氨基酸对血红素羧基进行40%-50%的修饰会降低修饰后血红素以及由这些血红素和珠蛋白重构的修饰后血红蛋白的过氧化物酶活性。血红蛋白衍生物催化活性的降低是由于修饰后血红素的过氧化物酶活性较低（与血红素相比）。因此得出结论，血红素羧基的氨基酸修饰不会影响血红蛋白分子中的血红素-蛋白质相互作用。
