Difference in rates of the reaction of various mammalian oxyhemoglobins with phenylhydrazine.
Arch Toxicol
; 69(3): 212-4, 1995.
Article
en En
| MEDLINE
| ID: mdl-7717880
ABSTRACT
Second order rate constants for the initial reaction of 12 mammalian oxyhemoglobins (Hb) with equimolar phenylhydrazine (PHZ), a compound inducing Heinz body hemolytic anemia, were determined by recording continuous changes in absorbance with time at 577 nm. The rate constants were varied in a range from 43 m-1.s-1 with pig Hb to 255 m-1.s-1 with dog Hb. On the other hand, isosbestic points at 526 and 587 nm were common to all the reaction processes. The aerobic reaction of Hb with PHZ resulted in denaturation of hemoprotein, and final reaction products were determined to be beta-meso-phenylbiliverdin IX alpha and N-phenylprotoporphyrin IX. These results suggest that the reactivity of PHZ to Hb is influenced by the globin molecule, and the oxidative cleavage of the porphyrin ring causes the denaturation of hemoprotein.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Fenilhidrazinas
/
Oxihemoglobinas
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Arch Toxicol
Año:
1995
Tipo del documento:
Article
País de afiliación:
Japón