Jump to main content
US EPA
United States Environmental Protection Agency
Search
Search
Main menu
Environmental Topics
Laws & Regulations
About EPA
Health & Environmental Research Online (HERO)
Contact Us
Print
Feedback
Export to File
Search:
This record has one attached file:
Add More Files
Attach File(s):
Display Name for File*:
Save
Citation
Tags
HERO ID
711038
Reference Type
Journal Article
Title
Structure-function alteration of hemoglobin in arsenicosis patients: A probable pathway to exert toxicity
Author(s)
Mondal, B; Chatterjee, D; Bhattacharyya, M
Year
2012
Is Peer Reviewed?
Yes
Journal
Journal of Applied Toxicology
ISSN:
0260-437X
EISSN:
1099-1263
Volume
32
Issue
8
Page Numbers
581-589
Language
English
PMID
21394736
DOI
10.1002/jat.1656
Web of Science Id
WOS:000305603100003
Abstract
Chronic arsenicosis, a major public health concern in India and Bangladesh, is mainly caused by ingestion of arsenic (As) contaminated ground water. Although this problem has been studied extensively, the mechanism of toxicity remains unknown. This paper investigates the process of trivalent arsenicals binding to hemoglobin (Hb) in chronic arsenicosis patients and consequent modification in the structure-function activity of Hb. In this work peroxidase activity, thermal denaturation profile, oxygen releasing capacity and hydrodynamic diameter have been evaluated for the Hb collected from subjects suffering with chronic arsenicosis. Increased peroxidative activity suggests altered oxidative status of Hb in the diseased state. The thermal denaturation profile indicates the Hb molecule to be more susceptible to unfolding in the pathologic state. The enhanced oxygen releasing capacity and significant reduction in hydrodynamic diameter of Hb is also observed in the diseased condition, suggesting conformational alterations in the Hb molecule. Finally, trivalent arsenic is found to bind with freshly isolated Hb from arsenicosis patients, binding affinity constant being 0.256 μM(-1) . The binding is positively cooperative with a Hill coefficient of +2.961 and isosbestic points at specific wavelengths. Thus, our work explores the structure-function property of Hb in chronic arsenicosis subjects and reveals that the molecule is modified in such a way that comparatively weak binding with oxygen and strong binding with arsenic occur simultaneously. This association may play a crucial role in exerting the pathway for arsenic toxicity. Copyright © 2011 John Wiley & Sons, Ltd.
Keywords
chronic arsenicosis; hemoglobin; peroxidative activity; thermal denaturation; oxygen release; hydrodynamic diameter; Hill coefficient
Tags
IRIS
•
Arsenic Hazard ID
1. Initial Lit Search
PubMed
WOS
ToxNet
WOS
Considered New
2. Lit Search Updates through Oct 2015
WOS
Considered
4. Considered through Oct 2015
5. Additions through Oct 2015
6. Cluster Filter through Oct 2015
7. Other Studies through Oct 2015
MOA
PBPK/TK
Noncancer MOA Seeds
•
Arsenic (Inorganic)
1. Literature
PubMed
Toxline, TSCATS, & DART
Web of Science
Lit search updates through Oct 2015
3. Hazard ID Screening
Other potentially supporting studies
4. Adverse Outcome Pathways/Networks Screening
Relevant
5. Susceptibility Screening
Excluded/Not relevant
•
Arsenic MOA
4. Adverse Outcome Pathways
ADME
1. MOA Literature Screening
MOA Seeds
MOA Cluster
Susceptibility Screening
•
Arsenic Susceptibility
5. Health Effect
Hematology, Hematopoietic System
1. Susceptibility Literature Screening
Keyword Search
2. Excluded
MOA/Mechanistic
3. References Identified During Review
Home
Learn about HERO
Using HERO
Search HERO
Projects in HERO
Risk Assessment
Transparency & Integrity