The rational use of mass spectrometry for amino acid sequence determination in peptides and extension of the possibilities of the method

  title={The rational use of mass spectrometry for amino acid sequence determination in peptides and extension of the possibilities of the method},
  author={M. M. Shemyakin and Y. Ovchinnikov and E. I. Vinogradova and A. Kiryushkin and M. Feigina and N. A. Aldanova and Y. Alakhov and V. Lipkin and A. I. Miroshnikov and B. V. Rosinov and S. A. Kazaryan},
  journal={FEBS Letters},
It has been shown earlier by us and by others that mass spectrometry can be used for the elucidation of the primary structure of peptides containing residues of all the ammo acids commonly found in proteins, N-acylpeptide esters being most suitable for this purpose (see [ 1,2] and references therein). Mass spectrometric determination of amino acid sequences is based on fragmentation of N-acylpeptide esters involving rupture of amide (ester) bonds and localization of the positive charge at the C… Expand
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The object chosen for study was the aspartate aminotransferase of the cytosol of pig heart; the enzyme, which is different from the mitochondrial isozyme, was prepared by a previously reported procedure. Expand
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A pressing problem in modern organic chemistry is the determination of the structure of polypeptides and proteins, for it is here that the needs and interests of biochemistry have far surpassedExpand
Mass spectrometry of N‐permethylated peptide derivatives; artifacts produced by C‐methylation
The Coggins-Benoiton procedure was adopted in the laboratory as the preferable method for Npermethylation, and was found to be successful for peptide sequence determination by mass spectrometry. Expand
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Comparison of the acetyl-, trifluoroacetyl-, benzyloxycarbonyl-, methoxycarbonyl-, ethoxycarbonyl, methylaminocarbonyl, phenylaminocarbonyl-, phthanoyl-, and stearoyl-derivatives ofExpand
Chemical and mass spectrometric sequence studies of a peptide from the variable part of normal immunoglobulin λ‐chains
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The revised structure of the peptide antibiotic esperin, established by mass spectrometry.
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