Geographic variation in blood plasma protein concentrations of young herring gulls (Larus argentatus) and Caspian terns (Sterna caspia) from the Great Lakes and Lake Winnipeg
Ka. Grasman et al., Geographic variation in blood plasma protein concentrations of young herring gulls (Larus argentatus) and Caspian terns (Sterna caspia) from the Great Lakes and Lake Winnipeg, COMP BIOC C, 125(3), 2000, pp. 365-375
Citations number
37
Categorie Soggetti
Pharmacology & Toxicology
Journal title
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY C-PHARMACOLOGY TOXICOLOGY & ENDOCRINOLOGY
Relative and total amounts of plasma protein fractions are affected by infe
ctions, inflammation, and nutritional and physiological status, and are the
refore important health indicators in free-living animals. Our objectives w
ere: (1) to examine intercolony differences in plasma protein fractions in
prefledgling gulls and terns; (2) to investigate relationships between plas
ma proteins and other physiological measures such as weight loss, growth, a
nd immune function; and (3) to examine potential associations between organ
ochlorine exposure and plasma proteins. During 1992, blood was collected fr
om 3-week-old herring gull (Larus argentatus) chicks from six sites on Lake
s Superior, Huron, Michigan, Erie, and Winnipeg acid from 3-week-old Caspia
n tern (Sterna caspia) chicks from five sites on Lakes Huron, Michigan, and
Ontario. These sites provided a wide gradient of organochlorine contaminat
ion. Plasma proteins were separated by high-resolution agarose gel electrop
horesis and stained with Coomassie brilliant blue dye. Six major fractions
were quantified: prealbumin, albumin, alpha-globulins, beta(1)-globulins, b
eta(2)-globulins, and gamma-globulins. Total protein, prealbumin, albumin,
and gamma-globulin concentrations and the albumin/globulin ratio did not di
ffer among sites. Total protein, albumin, and the albumin/globulin ratio we
re not decreased in birds experiencing food stress or weight loss. Intersit
e differences were found in alpha- and beta-globulins. In gulls, beta(2)-gl
obulins were positively associated with polychlorinated biphenyls (PCBs) an
d 1,1-dichloro-2,2-bis(p-chlorophenyl)ether (DDE). In terns, PCBs were nega
tively associated with alpha-globulins and positively associated with beta(
1)-globulins. Additional research is needed to identify individual proteins
and elucidate causal relationships between the particular protein concentr
ations and factors such as contaminants, growth, and condition. (C) 2000 El
sevier Science Inc. All rights reserved.