Document Detail

Comparison of NADH-dependent cytochrome b5 reductase activity and in vitro methemoglobin induction by sodium nitrite in Oncorhynchus mykiss, Salmo salar, and Salvelinus fontinalis.
MedLine Citation:
PMID:  23079863     Owner:  NLM     Status:  Publisher    
Methemoglobin is hemoglobin containing ferric iron. Methemoglobin cannot bind to oxygen and at high concentrations causes tissue hypoxia. Brook trout (Salvelinus fontinalis) develop significantly greater methemoglobinemia than Atlantic salmon (Salmo salar) or rainbow trout (Oncorhynchus mykiss) following general anesthesia with benzocaine or tricaine methanesulfonate. The objective of this study was to compare the activity of the major methemoglobin reducing enzyme, NADH-dependent cytochrome b5 reductase (CB5R), in brook trout erythrocytes to the activity of CB5R in Atlantic salmon and rainbow trout erythrocytes. Methemoglobin levels were compared using co-oximetry following in vitro incubation of erythrocytes with sodium nitrite (NaNO(2)). The CB5R activity was measured using a ferricyanide assay. There was significantly greater methemoglobin at time 0 in brook trout erythrocytes than in rainbow trout or Atlantic salmon erythrocytes (2.79 ± 0.29 %, 2.19 ± 0.23 %, 2.08 ± 0.14 %), (P < 0.001). There was significantly greater methemoglobin induction by NaNO(2) in brook trout erythrocytes (33.14 ± 3.32 %) than in rainbow trout or Atlantic salmon erythrocytes (28.73 ± 2.92 % and 24.85 ± 1.40 %, respectively), (P < 0.001). The CB5R activity was significantly less in brook trout erythrocytes (median of 3.05 μmol/min/μl) than in rainbow trout erythrocytes (median of 6.73 μmol/min/μl). The CB5R activity in Atlantic salmon erythrocytes (median 4.09 μmol/min/μl) was not significantly different than in brook or rainbow trout erythrocytes. Total methemoglobin at any one time is a balance between induction by oxidants and reduction by antioxidants. Lower CB5R activity in brook trout erythrocytes may contribute to a species-specific sensitivity to methemoglobin induction; however, there are likely additional factors.
Sandra McConkey; Janet Saunders; David J Speare
Related Documents :
11566363 - Patterns of adaptation in a laboratory evolved thermophilic enzyme.
22903323 - Three-stage extraction of gelatines from tendons of abattoir cattle: 1-reaction conditi...
4547783 - Substrates of hageman factor. i. isolation and characterization of human factor xi (pta...
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-10-19
Journal Detail:
Title:  Fish physiology and biochemistry     Volume:  -     ISSN:  1573-5168     ISO Abbreviation:  Fish Physiol. Biochem.     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-10-19     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100955049     Medline TA:  Fish Physiol Biochem     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Department of Biomedical Sciences, Atlantic Veterinary College, Charlottetown, PE, C1A 4P3, Canada,
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Graphene oxide strongly inhibits amyloid beta fibrillation.
Next Document:  Effect of supplemental oxygen on post-exercise inflammatory response and oxidative stress.