Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A.

Brown,; Hartley, B. S.

doi:10.1042/bj1010214

Cited by 451 publications

(159 citation statements)

References 16 publications

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“…The cross-linked products can then be analysed for composition by two-dimensional, 'diagonal' [3], SDS-polyacrylamide gel electrophoresis, in which the cross-links are cleaved between the first and second dimension steps. This procedure avoids any misinterpretations that could arise from identification of cross-linked species on the basis of electrophoretic mobility.…”

Section: Introductionmentioning

confidence: 99%

Cleavable cross‐links in the analysis of histone—histone associations

Thomas

Kornberg

1975

FEBS Letters

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Section: Introductionmentioning

confidence: 99%

Cleavable cross‐links in the analysis of histone—histone associations

Thomas

Kornberg

1975

FEBS Letters

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“…Identification of DNS-amino acids, amino acid analyses, high voltage paper electrophoresis, paper chromatography, peptide column chromatography on Dowex 50 X 4 and 1 X 2, and peptide sequencing were performed as described previously [5]. Diagonal methods were used for the selective purification of the cysteine peptide [ 13], and for the study of the methionine [14] and lysine [15] peptides.…”

Section: Introductionmentioning

confidence: 99%

Troponins C from reptile and fish muscles and their relation to muscular parvalbumins

Demaille¹,

Dutruge²,

Eisenberg

et al. 1974

FEBS Letters

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“…Mass spectral fragmentation in the negative ion mode of the peptides derived from trisulfides and tetrasulfides results in isulfide bonds are widely observed in naturally occurring peptides and proteins. Considerable effort has been spent on mass spectrometry based methods for establishing the presence and assigning the location of cysteine residues involved in the formation of disulfide bridges in natural polypeptides [1][2][3][4][5][6][7][8][9][10][11][12]. The presence of disulfide bridges in peptide natural products can be established under conditions of negative ion mass spectrometry with neutral loss of H 2 S 2 serving as a diagnostic.…”

mentioning

confidence: 99%

Characterization of alkali induced formation of lanthionine, trisulfides, and tetrasulfides from peptide disulfides using negative ion mass spectrometry

Thakur

Balaram

2009

J. Am. Soc. Mass Spectrom.

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Peptide disulfides are unstable under alkaline conditions, resulting in the formation of products containing lanthionine and polysulfide linkages. Electrospray ionization mass spectrometry has been used to characterize major species obtained when cyclic and acyclic peptide disulfides are exposed to alkaline media. Studies on a model cyclic peptide disulfide ͑Boc Ϫ Cys Ϫ Pro Ϫ Leu Ϫ Cys Ϫ NHMe͒ and an acyclic peptide, oxidized glutathione, bis C ( ␥ Glu -Cys -Gly -COOH), are described. Disulfide cleavage reactions are initiated by the abstraction of C ␣ H or C ␤ H protons of Cys residues, with subsequent elimination of H 2 S or H 2 S 2 . The buildup of reactive thiol species which act on intermediates containing dehydroalanine residues, rationalizes the formation of lanthionine and polysulfide products. In the case of the cyclic peptide disulfide, the formation of cyclic products is facilitated by the intramolecular nature of the Michael addition reaction of thiols to the dehydroalanine residue. Mass spectral evidence for the intermediate species is presented by using alkylation of thiol groups as a trapping method. Mass spectral fragmentation in the negative ion mode of the peptides derived from trisulfides and tetrasulfides results in isulfide bonds are widely observed in naturally occurring peptides and proteins. Considerable effort has been spent on mass spectrometry based methods for establishing the presence and assigning the location of cysteine residues involved in the formation of disulfide bridges in natural polypeptides [1][2][3][4][5][6][7][8][9][10][11][12]. The presence of disulfide bridges in peptide natural products can be established under conditions of negative ion mass spectrometry with neutral loss of H 2 S 2 serving as a diagnostic. Abstraction of the C ␣ -hydrogen results in formation of a peptide enolate at Cys residues, which can subsequently cleave to yield dehydroalanine residue with loss of H 2 S or H 2 S 2 . The use of negative ion mass spectrometry [13][14][15][16][17][18][19][20][21][22][23][24][25][26][27][28][29] for the study of disulfide containing peptide natural products has been established in an extensive series of investigations by Bowie and coworkers [30 -35] and other groups [36 -38]. During the course of recent attempts to fragment the negative ions of disulfide bridged peptides under mass spectrometric conditions, we noted that the cleavage reactions closely resemble those observed during breakage of disulfide bonds under alkaline conditions [39,40]. Under basic conditions, both ␣-and ␣ ␤-hydrogens of cysteine residues can be abstracted ␤ leading to two distinct modes of cleavage of the disulfide bonds, as noted by Parker and Kharasch in their comprehensive review of the mechanism of scission of sulfur-sulfur bonds [41]. The abstraction of an ␣-proton ␣ leads to the formation of a dehydroalanine residue and a persulfide, while abstraction of the ␤-proton results in ␤ formation of a thioaldehyde and a free thiol (cysteine). These processes are facile in both basic media ...

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Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A.

Cited by 451 publications

References 16 publications

Cleavable cross‐links in the analysis of histone—histone associations

Cleavable cross‐links in the analysis of histone—histone associations

Troponins C from reptile and fish muscles and their relation to muscular parvalbumins

Characterization of alkali induced formation of lanthionine, trisulfides, and tetrasulfides from peptide disulfides using negative ion mass spectrometry

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