The antigenic structure of the human glycoprotein hormone alpha-subunit: III. Solution- and solid-phase mapping using synthetic peptides

Twenty-seven synthetic peptides, representing the entire structure of the human glycoprotein hormone alpha-subunit were used to map the antigenic structure of the alpha-subunit. Solution phase and solid phase assays were performed with these peptides and a panel of eight monoclonal antibodies (MAb)....

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Bibliographic Details
Published inEndocrinology (Philadelphia) Vol. 128; no. 6; p. 2907
Main Authors Charlesworth, M C, Bergert, E R, Morris, J C, McCormick, D J, Ryan, R J
Format Journal Article
LanguageEnglish
Published United States 01.06.1991
Subjects
Antibodies, Monoclonal
Antigens - immunology
Enzyme-Linked Immunosorbent Assay
Glycoproteins - chemistry
Glycoproteins - immunology
Hormones - chemistry
Hormones - immunology
Humans
Peptide Mapping - methods
Peptides - chemical synthesis
Radioimmunoassay - methods
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Summary:Twenty-seven synthetic peptides, representing the entire structure of the human glycoprotein hormone alpha-subunit were used to map the antigenic structure of the alpha-subunit. Solution phase and solid phase assays were performed with these peptides and a panel of eight monoclonal antibodies (MAb). Two dominant regions were localized between residues 22-37 and 70-87. All eight antibodies recognized these regions, but differed somewhat with respect to whether they saw the more N-terminal, middle, or C-terminal portions of these regions. The sequence of residues 13-22 was recognized by three MAbs. The C-terminal region from residues 84-92 was recognized by three MAbs. All MAbs recognized conformational epitopes in that they reacted with two or more regions. Three MAbs (two against free alpha and one against human CG) have linear amino acid sequences as part of their conformational epitope.
ISSN:0013-7227
DOI:10.1210/endo-128-6-2907