A new mass-spectrometric C-terminal sequencing technique finds a similarity between γ-interferon and α2-interferon and identifies a proteolytically clipped γ-interferon that retains full antiviral activity

摘要: A novel mass-spectrometric technique is described that permits the identification of C-terminal peptide a protein. The involves incorporation 18O into all alpha-carboxy groups liberated during enzyme-catalysed partial hydrolysis protein, followed by mass spectrometry to identify as only did not incorporate any 18O. has been used true tryptic bacterially produced gamma-interferon and distinguish it from anomalous cleavage. It was found closely similar sequence segment alpha 2-interferon undergoes an analogous also C-terminus clipped retains full antiviral activity.