Conserved and Variant Molecular and Functional Features of Multiple Egg Yolk Precursor Proteins (Vitellogenins) in White Perch (Morone americana) and other Teleosts

Immunoglobulin Y (IgY) is the major antibody isotype in birds, reptiles, amphibia, and lungfish, playing a similar biological role as mammal IgG. Due to its phylogenetic distance, immune diversification and presence in the egg yolk, IgY provide a number of advantages in immunodiagnostic compared to IgG from mammals. Moreover, IgY production is in agreement with international efforts to reduce, refine and if possible, to replace animals in experimentation, contributing substantially in favor of animal welfare. This article presents an overview about structural and functional features, production and applications of IgY in immunodiagnostic, as well as the advantages of chicken antibodies use.

Download Full-text

Lethal and sublethal exposure and recovery effects of ozone-produced oxidants on adult white perch (Morone americana Gmelin)

Water Research ◽

10.1016/0043-1354(83)90101-x ◽

1983 ◽

Vol 17 (2) ◽

pp. 205-213 ◽

Cited By ~ 19

Author(s):

Leonard B. Richardson ◽

Dennis T. Burton ◽

Ronald M. Block ◽

Ann M. Stavola

Keyword(s):

White Perch ◽

Morone Americana ◽

Sublethal Exposure

Download Full-text

Effect of acute and chronic temperature transition on enzymes of cardiac metabolism in white perch (Morone americana), yellow perch (Perca flavescens), and smallmouth bass (Micropterus dolomieui)

Canadian Journal of Zoology ◽

10.1139/z91-040 ◽

1991 ◽

Vol 69 (1) ◽

pp. 258-262 ◽

Cited By ~ 30

Author(s):

Dawn H. Sephton ◽

William R. Driedzic

Keyword(s):

Yellow Perch ◽

Citrate Synthase ◽

White Perch ◽

Perca Flavescens ◽

Smallmouth Bass ◽

Transferase Activity ◽

Morone Americana ◽

Coa Transferase ◽

Micropterus Dolomieui ◽

The Impact

White perch (Morone americana), yellow perch (Perca flavescens), and smallmouth bass (Micropterus dolomieui) were acclimated to 5 and 20 °C. There was an increase in ventricle mass relative to body mass in smallmouth bass only following acclimation to 5° C. Maximal in vitro activities of hexokinase, citrate synthase, carnitine acyl CoA transferase (with palmitoyl CoA, palmitoleoyl CoA, and oleoyl CoA as substrates), and total ATPase were assessed in crude heart homogenates. Tissues removed from warm-acclimated animals were tested at 20 and 5 °C; tissues removed from cold-acclimated animals were assessed at 5 °C. Acute temperature transitions were associated with decreases in the activities of hexokinase (Q10 ≈ 1.8), citrate synthase (Q10 ≈ 1.4), and ATPase (Q10 ≈ 1.7). The impact of temperature on carnitine acyl CoA transferases was generally less severe. This suggests that maximal fatty acid oxidation is conserved better than glucose oxidation during a warm to cold transition. Maximal enzyme activities were generally unaffected by the acclimation regime, with the exception of that of carnitine acyl CoA transferase in white perch heart. The substantial increase in carnitine acyl CoA transferase activity when unsaturated CoA derivatives were provided as substrate suggests an increased capacity to oxidize unsaturated fatty acids at low temperature following an acclimation period. Attempts to sustantiate this contention by offering labelled oleic acid to ventricle sheets were thwarted by a high rate of incorporation into the total lipid pool.

Download Full-text