[44] Cleavage of the tryptophanyl peptide bond by dimethyl sulfoxide-hydrobromic acid

Savige, W. E.; Fontana, Angelo

doi:10.1016/0076-6879(77)47046-0

Cited by 50 publications

(29 citation statements)

References 34 publications

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“…A small amount of a peptide fragment starting with Lys-43 was also observed. This fragment may have been generated by chemical cleavage at Trp-42 during the strongly acidic treatment of the protein in the presence of sulfoxide (i.e., methionine oxide) (31). HPLC analysis was consistent with a major component or group of closely related peptides.…”

Section: Methodsmentioning

confidence: 70%

Chemical synthesis and enzymatic activity of a 99-residue peptide with a sequence proposed for the human immunodeficiency virus protease.

Nutt

Brady

Darke

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

104

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Retroviral proteins, including those from the human immunodeficiency virus (HIV), are synthesized as polyprotein precursors that require proteolytic cleavage to yield the mature viral proteins. A 99-residue polypeptide, encoded by the 5' end of the pol gene, has been proposed as the processing protease of HIV. The chemical synthesis of the 99-residue peptide was carried out by the solid-phase method, and the isolated product was found to exhibit specific proteolytic activity upon folding under reducing conditions. Upon size-exclusion chromatography, enzymatic activity was eluted at a point consistent with a dimeric molecular size. Specificity was demonstrated by the cleavage of the natural substrate HIV gag p55 into gag p24 and gag p17, as well as cleavage of small peptide substrates representing processing sites of HIV fusion proteins. The proteolytic action of the synthetic product could be inhibited by pepstatin, an aspartic protease inhibitor.

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Section: Methodsmentioning

confidence: 70%

Chemical synthesis and enzymatic activity of a 99-residue peptide with a sequence proposed for the human immunodeficiency virus protease.

Nutt

Brady

Darke

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

104

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“…As to oxidative stress, this could be very useful to analyze oxidation of aromatic amino acids. As a matter of fact, many :classical methods for chemical cleavage after aromatic amino acids (Tyr or Trp), start with the oxidation of the amino acids, followed by a cleavage step that uses the reactivity of the oxidized amino acid [57,58]. The use of the sole cleavage step could provide an efficient tool to localize oxidized aromatic amino acids.…”

Section: Five-year Viewmentioning

confidence: 99%

Oxidative stress response: a proteomic view

Rabilloud¹,

Chevallet²,

Luche³

et al. 2005

Expert Review of Proteomics

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The oxidative stress response is characterized by various effects on a range of biological molecules. When examined at the protein level, both expression levels and protein modifications are altered by oxidative stress. While these effects have been studied in the past by classical biochemical methods, the recent onset of proteomics methods have allowed to study the oxidative stress response on a much wider scale. The input of proteomics in the study of oxidative stress response or in the evidence of an oxidative stress component in biological phenomena is thus reviewed in this paper. 3/2107/ 07/2008, 17:07:49

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“…b Calculated from the amino acid sequence [2]. ¢ Tyr and Trp residues of the peptides were modified to 3-bromotyrosyl and N-acyl-dioxoindolylalanyllactone derivatives [10].…”

Section: Resultsmentioning

confidence: 99%

Primary structure and catalytic properties of extracellular ribonuclease of bacillus circulans

1993

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[44] Cleavage of the tryptophanyl peptide bond by dimethyl sulfoxide-hydrobromic acid

Cited by 50 publications

References 34 publications

Chemical synthesis and enzymatic activity of a 99-residue peptide with a sequence proposed for the human immunodeficiency virus protease.

Chemical synthesis and enzymatic activity of a 99-residue peptide with a sequence proposed for the human immunodeficiency virus protease.

Oxidative stress response: a proteomic view

Primary structure and catalytic properties of extracellular ribonuclease of bacillus circulans

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