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- Title
Solid--Phase Synthesis of the Non--Calcium--Binding Loop of Cod Allergen M Direct Evidence of the Reactivity of the Amino--Terminal Segment.
- Authors
Elsayed, S.; Ragnarsson, U.; Nethland, B.
- Abstract
The synthesis of the non-calcium-binding AB loop of the assembly 13-32 of cod Allergen M (Mr 2122.1) was accomplished by solid-phase peptide synthesis. This peptide and the previously synthesized ones [12, 13, 14] have significant amino acid sequence homology. The synthetic crude preparation was obtained at relatively high recovery and purity. Further purification on a Bio-Gel P-2 column and a reversed-phase high-performance liquid chromatography column improved the grade of homogeneity, as demonstrated by high-voltage electrophoresis end-terminal analysis, and amino acid composition. The peptide could, although to a much weaker extent than the intact Allergen M. directly hind IgE antibodies from the sera of cod-ailergic individuals. At identical molar concentrations, a ratio of 1 :6 for the in vitro reactivity of the peptide relative to the intact Allergen M was obtained. A similar reactivity was shown in the in vivo system used. The peptide also reacted with rabbit anti-Allergen M antibodies in rocket immunoelectrophoresis. The peptide appears to function as a divalent molecule in its primary interaction with antibodies.
- Subjects
PEPTIDE synthesis; IMMUNOGLOBULINS; AMINO acid sequence; HOMOLOGY (Biology); IMMUNOELECTROPHORESIS; SERUM
- Publication
Scandinavian Journal of Immunology, 1983, Vol 17, Issue 3, p291
- ISSN
0300-9475
- Publication type
Article
- DOI
10.1111/j.1365-3083.1983.tb00792.x