Practical Protein Chemistry - A. Darbre 1989

Application of electron impact mass spectrometry for determining the amino acid sequence of peptides and proteins
Introduction

A. DELL (Department of Biochemistry, Imperial College of Science and Technology, London SW7 2AZ, U.K.)

This chapter discusses the methodology and practical results of determining the Amino Acid Sequence of peptide mixtures subjected to Acetylation and methylation using low-resolution Electron Impact Mass Spectrometry. This approach has been successfully employed to determine the Introduction/19.html">Primary Structure of A number of Proteins, such as ribitol dehydrogenase [1], chloramphenicol acetyltransferase [2, 3], Pseudomonas azurin [4], and Dihydrofolate Reductase from L. casei (the only protein whose complete amino acid sequence was determined solely by mass spectrometry) [5, 6], as well as Peptides whose Amino acid sequences could not be established by classical Protein Chemistry Methods due to the presence of N-terminal blocking groups, Unusual amino acid residues within the chain, severe difficulties associated with the isolation of individual substances, or other reasons [7—15].



Last update: 06/08/2026

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