Solid‐Phase Synthesis of the Non‐Calcium‐Binding Loop of Cod Allergen M

Publisher Website
Google Scholar
Abstract
The synthesis of the non‐calcium‐binding AB loop of the assembly 13–32 of cod Allergen M (M r 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 bind IgE antibodies from the sera of cod‐allergic 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.