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Serum proteins in the leopard seal, Hydrurga leptonyx, in Prydz Bay, Eastern Antarctica and the coast of NSW, Australia.

Authors :
Gray R
Canfield P
Rogers T
Source :
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology [Comp Biochem Physiol B Biochem Mol Biol] 2005 Sep; Vol. 142 (1), pp. 67-78.
Publication Year :
2005

Abstract

Blood protein analysis including total serum protein and albumin by chemical methods, fibrinogen estimation and serum protein electrophoresis (SPE) was performed on the leopard seal, Hydrurga leptonyx. The most commonly observed SPE pattern was eight fractions designated albumin, alpha(1a), alpha(1b), alpha(2a), alpha(2b), beta(1), beta(2) and gamma-globulin. Significantly higher total serum protein and albumin concentrations, as determined by chemical methods, and significantly higher alpha(2)-globulin concentrations, determined by SPE, were seen in free-ranging male seals compared to females, whilst significantly higher beta-globulin concentrations were seen in female seals. Season of sampling influenced fibrinogen and beta(2)-globulin concentrations, whereas there were no significant differences in any protein concentrations with moult status. Qualitative comparison of SPE traces of leopard seals in Antarctica with "sick" individuals in NSW, Australia revealed obvious differences, as did quantitative comparison of protein concentrations where differences in alpha(1), alpha(2), beta(1), beta(2), and gamma-globulin concentrations were seen. These findings suggest that SPE is a useful tool for investigating serum proteins in the leopard seal, with applications for the investigation of "sick" individuals and the assessment of variation in homeostasis. This technique could also be used to identify the presence of environmental stressors, subclinical disease and physiological variation within specific seal populations.

Details

Language :
English
ISSN :
1096-4959
Volume :
142
Issue :
1
Database :
MEDLINE
Journal :
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology
Publication Type :
Academic Journal
Accession number :
15993637
Full Text :
https://doi.org/10.1016/j.cbpc.2005.05.016