Chemical Characterization of a Non-Covalently Linked Peptide from Plakalbumin

Abstract

A 33·residue peptide isolated from plakalbumin by dissociation with urea at pH 3 is shown to be derived from the a-terminal portion of ovalbumin. The yield of proline obtained on hydrazinolysis was the same as that from ovalbumin, whereas proline was not liberated from the protein component. The N·terminal sequence of this peptide was determined by the Edman degradative procedure to be Ser. V al.Ser .Glu.Glu.Phe.Arg.Ala.Asp.