Isolation and Properties of An Immunoreactive Glycopeptide Connecting First and Second Domains of Chicken Ovomucoid

Abstract

A glycopeptide was isolated from a peptic hydrolysate of chicken ovomucoid using gel filtration after reduction with 2-mercaptoethanol. The glycopeptide was thought to be derived from the sequence Gly⁵¹-Tyr⁷³ of chicken ovomucoid and retained the immunoreactivity to IgG of mouse antiserum and IgE of human serum specific to ovomucoid. About fifty percent of the immunoreactivity to mouse antiserum was inhibited by the sera of patients allergic to ovomucoid and also by the carbohydrate chains on ovomucoid. These results suggested that the glycopeptide, connecting the first domain and second domain of chicken ovomucoid, participated in egg allergy, and the ovomucoid carbohydrate chains contributed to the immunoreactivity of the glycopeptide.