Development and immunochemical evaluation of antibodies Y for the poorly immunogenic polypeptide prothymosin alpha

Since conserved mammalian polypeptides are believed to exhibit enhanced immunogenicity in avian species, hens were immunized against the poorly immunogenic, highly conserved mammalian polypeptide prothymosin alpha (ProTα), i.e. against either non-conjugated ProTα (isolated from bovine thymus) or Pro...

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Bibliographic Details
Published in:Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2006, Vol.27 (1), p.183-193
Main Authors: Klimentzou, Persefoni, Paravatou-Petsotas, Maria, Zikos, Christos, Beck, Alexander, Skopeliti, Margarita, Czarnecki, Jan, Tsitsilonis, Ourania, Voelter, Wolfgang, Livaniou, Evangelia, Evangelatos, Gregory P.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Biological and medical sciences
Cattle
Chickens - immunology
Female
Fundamental and applied biological sciences. Psychology
HeLa Cells
Hemocyanins - immunology
Hemocyanins - metabolism
Hen antibodies Y
Highly conserved mammalian polypeptides
Humans
Immunoblotting
Immunoglobulin G - biosynthesis
Immunoglobulin G - chemistry
Immunoglobulin G - isolation & purification
Immunoglobulin Heavy Chains - isolation & purification
Immunoglobulin Light Chains - isolation & purification
Immunoglobulins - biosynthesis
Immunoglobulins - chemistry
Immunoglobulins - isolation & purification
Molecular Sequence Data
Peptide Fragments - chemistry
Peptide Fragments - immunology
Protein Precursors - immunology
Protein Precursors - metabolism
Prothymosin alpha
Prothymosin alpha conjugated to keyhole limpet hemocyanin
Rabbit antibodies G
Rabbits
Thymosin - analogs & derivatives
Thymosin - immunology
Thymosin - metabolism
Vertebrates: endocrinology
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Summary:Since conserved mammalian polypeptides are believed to exhibit enhanced immunogenicity in avian species, hens were immunized against the poorly immunogenic, highly conserved mammalian polypeptide prothymosin alpha (ProTα), i.e. against either non-conjugated ProTα (isolated from bovine thymus) or ProTα conjugated to keyhole limpet hemocyanin (ProTα/KLH). The antibodies Y were isolated from the egg yolk and evaluated through suitable dot-blot and ELISA systems in parallel with antibodies G isolated from the antiserum of rabbits immunized against the same immunogens. As revealed, antibodies Y and G of low titer and/or affinity were obtained against non-conjugated ProTα, while antibodies Y against ProTα/KLH had a better apparent titer, could better discriminate between ProTα and the closely related bioactive peptide thymosin alpha 1, and were obtained at much larger quantities than the corresponding antibodies G.
ISSN:0196-9781
1873-5169
DOI:10.1016/j.peptides.2005.07.002