Computation of Amino Acid Sequences of Polypeptides from Masses of Their Constituent Peptide Fragments and Amino Acid Residues Released in Edman-degradation

Kitagishi, Toyoko; Hong, Yeong‐Man; Takao, Toshifumi; Aimoto, Saburo; Shimonishi, Yasutsugu

doi:10.1246/bcsj.55.575

Cited by 8 publications

(1 citation statement)

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“…Subsequently, diverse approaches using data obtained from unfractionated protein digests have been reported (Fairwell et al, 1970;Cannon and Lovins, 1972;Biemann, 1980;Matsuo et al, 1981;Kitagishy et al, 1981Kitagishy et al, , 1982Shimonishi et aL, 1981;Herlihy and Biemann, 1981;Erickson and Jardine, 1986). These methods, revised by Petrilli and Colosimo (1990), are based on the use of mass spectrometry, a technique well suited for working on peptide mixtures.…”

Section: Introductionmentioning

confidence: 99%

Determination of the primary structure of homologous proteins by sequence analysis of peptide mixtures

1996

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We propose a rapid method to determine the primary structure of a protein knowing the sequence of a homologous protein. The method consists in submitting both the reduced and alkylated proteins to an enzymatic or chemical hydrolysis and performing the sequence analysis of the peptide mixtures. The assessment of the unknown sequence and the degree of identify of the two proteins are reached by comparing the two sequence analyses. The sequences of all the possible peptides present in the two mixtures are reconstructed and the differences in the two sequences are determined. If necessary, the differences can be confirmed by performing a mass spectrometric analysis of the two mixtures. We used this procedure on two homologous proteins of known sequence to furnish an application example of the method.

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Section: Introductionmentioning

confidence: 99%

Determination of the primary structure of homologous proteins by sequence analysis of peptide mixtures

1996

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Simultaneous analysis of C-terminal amino acid residues of peptide mixtures by combination of field desorption mass spectrometry and carboxypeptidase digestion

Hong

Takao

Aimoto

et al. 1983

Biol. Mass Spectrom.

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A novel method is described for the simultaneous analysis of C-terminal amino acid residues of peptide mixtures by combination of field desorption mass spectrometry and carboxypeptidase digestion. The method involves measurement of the mass values of quasi-molecular ions ([M+H]') of peptides and their digested fragments. The amino acid residues can he determined from the mass differences of the mass values observed in the field desorption mass spectra during digestion of peptides. As typical examples, the simultaneous determinations of the C-terminal amino acid residues of peptide mixtures prepared by tryptic digestion of P-endorphin and parathyroid peptide are described.

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Characterization of extracellular proteases from Trametes trogii

et al. 1996

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Computation of Amino Acid Sequences of Polypeptides from Masses of Their Constituent Peptide Fragments and Amino Acid Residues Released in Edman-degradation

Cited by 8 publications

References 9 publications

Determination of the primary structure of homologous proteins by sequence analysis of peptide mixtures

Determination of the primary structure of homologous proteins by sequence analysis of peptide mixtures

Simultaneous analysis of C-terminal amino acid residues of peptide mixtures by combination of field desorption mass spectrometry and carboxypeptidase digestion

Characterization of extracellular proteases from Trametes trogii

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