Characterization of Antibodies Against Human N-Terminal Parathyroid Hormone by Epitope Mapping

Two polyclonal antisera from goat and mouse and two monoclonal antibodies against human parathyroid hormone (1-34) were characterised by epitope mapping. Hexapeptides were synthesized on polystyrene pins, the sequences of which overlapped and represented the entire sequence of hPTH(1-34). Binding of...

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Veröffentlicht in:	Journal of immunoassay (Monticello, N.Y.) N.Y.), 1992-03, Vol.13 (1), p.1-13
Hauptverfasser:	Tampe, Jens, Broszio, Pia, Manneck, Hans E., Mißbichler, Albert, Blind, Eberhard, Müller, Karen B., Schmidt-Gayk, Heinrich, Armbruster, Franz Paul
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Antibodies Antibodies, Monoclonal Biological and medical sciences epitope mapping Epitopes - chemistry Fundamental and applied biological sciences. Psychology Fundamental immunology Humans Immunochemistry Models, Molecular Molecular immunology Molecular Sequence Data monoclonal antibodies parathyroid hormone Parathyroid Hormone - chemistry Parathyroid Hormone - immunology Peptide Fragments - chemistry Peptide Fragments - immunology Peptide Mapping Protein Conformation Techniques Teriparatide
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Beschreibung
Zusammenfassung:	Two polyclonal antisera from goat and mouse and two monoclonal antibodies against human parathyroid hormone (1-34) were characterised by epitope mapping. Hexapeptides were synthesized on polystyrene pins, the sequences of which overlapped and represented the entire sequence of hPTH(1-34). Binding of antibodies to these hexapeptides was determined and antigenic determinants thus characterized. At least one predominant binding sequence was detected in the region of hPTH(7-14).
ISSN:	0197-1522 2332-4090
DOI:	10.1080/15321819208019821