Hemoglobins Likely Function as Peroxidase in Blood Clam Tegillarca granosa Hemocytes
| Autor: | Wang Sufang, Yongbo Bao, Xiaopei Yu, Qinggang Xue, Shunqin Zhang, Zhihua Lin, Liangyi Xue |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Tegillarca granosa lcsh:Immunologic diseases. Allergy Article Subject biology Immunology General Medicine biology.organism_classification Horseradish peroxidase 03 medical and health sciences chemistry.chemical_compound 030104 developmental biology 0302 clinical medicine Biochemistry chemistry Myeloperoxidase biology.protein Urea Immunology and Allergy Sodium azide Hemoglobin lcsh:RC581-607 Heme 030217 neurology & neurosurgery Peroxidase |
| Zdroj: | Journal of Immunology Research, Vol 2017 (2017) |
| ISSN: | 2314-7156 2314-8861 |
| Popis: | Hemoglobins are a group of respiratory proteins principally functioning in transport of oxygen and carbon dioxide in red blood cells of all vertebrates and some invertebrates. The blood clamT. granosais one of the few invertebrates that have hemoglobin-containing red hemocytes. In the present research, the peroxidase activity ofT. granosahemoglobins (Tg-Hbs) was characterized and the associated mechanism of action was deciphered via structural comparison with other known peroxidases. We detected that purified Tg-Hbs catalyzed the oxidation of phenolic compounds in the presence of exogenous H2O2. Tg-Hbs peroxidase activity reached the maximum at pH 5 and 35°C and was inhibited by Fe2+, Cu2+, SDS, urea, and sodium azide. Tg-Hbs shared few similarities in amino acid sequence and overall structural characteristics with known peroxidases. However, the predicted structure at their heme pocket was highly similar to that of horseradish peroxidase (HRP) and myeloperoxidase (MPO). This research represented the first systemic characterization of hemoglobin as a peroxidase. |
| Databáze: | OpenAIRE |
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