Hemoglobin as a major binding protein for methylmercury in white-sided dolphin liver.
about
Synthesis, characterization, DFT calculations, and electrochemical comparison of novel iron(ii) complexes with thione and selone ligands.Mercury Exposure: Protein Biomarkers of Mercury Exposure in Jaraqui Fish from the Amazon Region.Pushing back the frontiers of mercury speciation using a combination of biomolecular and isotopic signatures: challenge and perspectives.Investigating the adduct formation of organic mercury species with carbonic anhydrase and hemoglobin from human red blood cell hemolysate by means of LC/ESI-TOF-MS and LC/ICP-MS.Remarkable differences in the biochemical fate of Cd2+, Hg2+, CH3Hg+ and thimerosal in red blood cell lysate.Natural Hg isotopic composition of different Hg compounds in mammal tissues as a proxy for in vivo breakdown of toxic methylmercury.
P2860
Hemoglobin as a major binding protein for methylmercury in white-sided dolphin liver.
description
2013 nî lūn-bûn
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2013年の論文
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2013年学术文章
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2013年学术文章
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2013年学术文章
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2013年学术文章
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2013年学术文章
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name
Hemoglobin as a major binding protein for methylmercury in white-sided dolphin liver.
@en
Hemoglobin as a major binding protein for methylmercury in white-sided dolphin liver.
@nl
type
label
Hemoglobin as a major binding protein for methylmercury in white-sided dolphin liver.
@en
Hemoglobin as a major binding protein for methylmercury in white-sided dolphin liver.
@nl
prefLabel
Hemoglobin as a major binding protein for methylmercury in white-sided dolphin liver.
@en
Hemoglobin as a major binding protein for methylmercury in white-sided dolphin liver.
@nl
P2093
P2860
P50
P1476
Hemoglobin as a major binding protein for methylmercury in white-sided dolphin liver
@en
P2093
Ryszard Lobinski
Sandra Mounicou
Zoyne Pedrero Zayas
P2860
P2888
P304
P356
10.1007/S00216-013-7274-6
P407
P577
2013-08-13T00:00:00Z