Abstract
Abstract: A chemical approach for selectively isolating the C-terminal peptide from a protein is described. The protein to be analyzed is derivatized with glycinamide to protect carboxyl groups at both C-terminus and Asp/Glu side chains and subsequently fragmented with protease. The resulting peptides are treated with a Sepharose-based resin, EAH Sepharose 4B which binds all fragments except the C-terminal peptide, through the formation of amide bonds. The unbound C-terminal peptide is purified by HPLC and identified using Edman sequencing and mass spectrometry analyses.
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