Document Detail


Astaxanthin binding protein in Atlantic salmon.
MedLine Citation:
PMID:  16644255     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The rubicund pigmentation in salmon and trout flesh is unique and is due to the deposition of dietary carotenoids, astaxanthin and canthaxanthin in the muscle. The present study was undertaken to determine which protein was responsible for pigment binding. Salmon muscle proteins were solubilized by sequential extractions with non-denaturing, low ionic strength aqueous solutions and segregated as such into six different fractions. Approximately 91% of the salmon myofibrillar proteins were solubilized under non-denaturing conditions using a protocol modified from a method described by Krishnamurthy et al. [Krishnamurthy, G., Chang, H.S., Hultin, H.O., Feng, Y., Srinivasan, S., Kelleher. S.D., 1996. Solubility of chicken breast muscle proteins in solutions of low ionic strength. J. Agric. Food Chem. 44: 408-415.] for the dissolution of avian muscle. To our knowledge, this is the first time this solubilization approach has been applied to the study of molecular interactions in myofibrillar proteins. Astaxanthin binding in each fraction was determined using an in vitro binding assay. In addition, SDS-PAGE and quantitative densitometry were used to separate and determine the relative amounts of each of the proteins in the six fractions. The results showed that alpha-actinin was the only myofibrillar protein correlating significantly (P<0.05) with astaxanthin binding. Alpha-actinin was positively identified using electrophoretic techniques and confirmed by tandem mass spectroscopy. Purified salmon alpha-actinin bound synthetic astaxanthin in a molar ratio of 1.11:1.00. The study was repeated using halibut alpha-actinin, which was found to have a molar binding ratio of astaxanthin to alpha-actinin of 0.893:1. These results suggest that the difference in pigmentation between white fish and Atlantic salmon is not due to binding capacity in the muscle, but rather differences in the metabolism or transport of pigment.
Authors:
Sarah J Matthews; Neil W Ross; Santosh P Lall; Tom A Gill
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-03-06
Journal Detail:
Title:  Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology     Volume:  144     ISSN:  1096-4959     ISO Abbreviation:  Comp. Biochem. Physiol. B, Biochem. Mol. Biol.     Publication Date:  2006 Jun 
Date Detail:
Created Date:  2006-05-22     Completed Date:  2006-08-03     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9516061     Medline TA:  Comp Biochem Physiol B Biochem Mol Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  206-14     Citation Subset:  IM    
Affiliation:
Department of Food Science and Technology, Dalhousie University, P.O. Box 1000, Halifax, Nova Scotia, Canada B3J 2X4.
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MeSH Terms
Descriptor/Qualifier:
Actinin / isolation & purification
Amino Acid Sequence
Animals
Electrophoresis, Polyacrylamide Gel
Flounder / physiology
Mass Spectrometry
Molecular Sequence Data
Muscles / chemistry
Pigmentation / physiology*
Pigments, Biological / isolation & purification
Protein Binding / physiology*
Salmo salar / physiology*
Xanthophylls / metabolism
Chemical
Reg. No./Substance:
0/Pigments, Biological; 0/Xanthophylls; 11003-00-2/Actinin; 472-61-7/astaxanthine

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


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