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.
journal_name
Arch Toxicoljournal_title
Archives of toxicologyauthors
Kinuta M,Matteson JL,Itano HAdoi
10.1007/s002040050161subject
Has Abstractpub_date
1995-01-01 00:00:00pages
212-4issue
3eissn
0340-5761issn
1432-0738journal_volume
69pub_type
杂志文章abstract::Cytokeratins (CK) constitute a family of cytoskeletal intermediate filament proteins that are typically expressed in epithelial cells. An abnormal structure and function are effects that are clearly related to liver diseases as non-alcoholic steatohepatitis, cirrhosis and hepatocellular carcinoma. We have previously o...
journal_title:Archives of toxicology
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