Literature DB >> 7115084

Mercury oxidation in vitro by ferric compounds.

M Ogata, K Kenmotsu, N Hirota, H Aikoh.   

Abstract

Among the ferric compounds studied, cytochrome C, methemoglobin, lactoperoxidase, ferritin and ferric ion, in addition to catalase, had the ability to oxidize metallic mercury in the presence of hydrogen peroxide. On the other hand, hematin, the active center of catalase, did not oxidize metallic mercury. The results are consistent with the increased oxidation and uptake of mercury in the liver by acatalasemia mice.

Entities:  

Mesh:

Substances:

Year:  1982        PMID: 7115084     DOI: 10.1007/bf00569242

Source DB:  PubMed          Journal:  Arch Toxicol        ISSN: 0340-5761            Impact factor:   5.153


  4 in total

Review 1.  Catalase: Physical and chemical properties, mechanism of catalysis, and physiological role.

Authors:  A Deisseroth; A L Dounce
Journal:  Physiol Rev       Date:  1970-07       Impact factor: 37.312

2.  Role of catalase in the oxidation of mercury vapor.

Authors:  L Magos; S Halbach; T W Clarkson
Journal:  Biochem Pharmacol       Date:  1978-05-01       Impact factor: 5.858

3.  Mercury uptake by acatalasemia mice and their erythrocytes, lung and liver homogenates.

Authors:  M Ogata; M Ikeda
Journal:  Int Arch Occup Environ Health       Date:  1978-03-15       Impact factor: 3.015

4.  In vitro mercury uptake by human acatalasemic erythrocytes.

Authors:  M Ogata; M Ikeda
Journal:  Arch Environ Health       Date:  1979 Jul-Aug
  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.