Sulfenyl halides as modifying reagents for polypeptides and proteins.  I.  Modification of tryptophan residues

Scoffone, Ernesto; Fontana, Angelo; Rocchi, Raniero

doi:10.1021/bi00843a014

Cited by 219 publications

(101 citation statements)

References 37 publications

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“…2) one expected to generate three derivatives, two monoderivatives and one bis-derivative, using appropriate relative concentrations of notexin and the indole side-chain reagent, 2-nitrophenylsulfenyl chloride (0,NPhS-C1) [27,30]. However, modification of notexin with 02NPhS-C1 led to two derivatives only.…”

Section: Discussionmentioning

confidence: 99%

“…Chemical modification of tryptophan residues of notexin was carried out according to Scoffone et al [27]. Notexin (160 nmol) was dissolved in 1 ml of acetic acid/water ( l / l ; by vol.)…”

Section: Prepara T Ion Of No Texin Derivativesmentioning

confidence: 99%

“…Elution was performed with a linear gradient of CH3CN in 0.1% trifluoroacetic acid at a flow rate of 1 .O ml/min. NP and Ns correspond respectively to the components designated in the text as notechis NP and notechis Ns duces a chromophore into proteins containing tryptophan, with an absorption band centered at 365 nm and a corresponding molar absorption coefficient ( E ) of 4000 M-' cm-' [27]. This chromophore provides a convenient quantitative measure of the extent of the reaction [30].…”

Section: Derivatization Of Notexin With 2-nitrophenylsulfenylchloridementioning

confidence: 99%

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Tryptophan 110, a residue involved in the toxic activity but not in the enzymatic activity of notexin

Mollier¹,

Chwetzoff²,

Bouet³

et al. 1989

European Journal of Biochemistry

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We prepared two derivatives of notexin, a phospholipase A2 from Motechis scutatus scutatus venom, by modifying the protein with 2-nitrophenylsulfenylchloride, a tryptophan-specific reagent. One derivative was modified at both tryptophans 20 and 110 whereas the other was modified at tryptophan 20. Evidence based on circular dichroic analysis and antigenicity towards a notexin-specific monoclonal antibody indicated that derivatization at both tryptophans did not affect the tertiary structure of notexin. Concomitant modification of tryptophans 20 and 110 induced a marked decrease in the capacity of notexin to kill mice and to block neuromuscular transmission in the chick biventer cervicis preparation, whereas selective modification at tryptophan 20 had no effect on the lethal properties of notexin. This implies that the decrease in the lethal properties of notexin after derivatization was due to modification at tryptophan 110. However, the diderivatized notexin retained full enzymatic activity, implying that neither tryptophan 20 and tryptophan 110 are involved in the catalytic function of the molecule. We conclude that notexin harbours two functional sites. One of them corresponds to the enzymatic site, whereas the other, which includes tryptophan 110, provides specific toxic characteristics to notexin. By reference to previous crystallographic studies, the relative spatial positions of elements involved in toxicity and the catalytic site, we propose a possible orientation of notexin with respect to its putative membrane-bound target.

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Section: Discussionmentioning

confidence: 99%

“…Chemical modification of tryptophan residues of notexin was carried out according to Scoffone et al [27]. Notexin (160 nmol) was dissolved in 1 ml of acetic acid/water ( l / l ; by vol.)…”

Section: Prepara T Ion Of No Texin Derivativesmentioning

confidence: 99%

Section: Derivatization Of Notexin With 2-nitrophenylsulfenylchloridementioning

confidence: 99%

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Tryptophan 110, a residue involved in the toxic activity but not in the enzymatic activity of notexin

Mollier¹,

Chwetzoff²,

Bouet³

et al. 1989

European Journal of Biochemistry

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“…Glucagon contains no cysteine and only the tryptophan residue was modified. Sulfenyl chlorides also are known to react with sulfhydryls (35,36). Guanidino Groups.…”

Section: Chemical Modification Of Proteinsmentioning

confidence: 99%

Chemical Modification of Proteins: An Overview

Feeney

Yamasaki

Geoghegan

1982

Advances in Chemistry

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“…The tryptophan content was determined by two independent methods [14,15]. The quantity of tryptophan per pmole of peptide (as determined by analysis of lysine and arginine content on the analyzer) corresponded in both cases to one residue.…”

Section: Amino Acid Analysis Of Fragment Cb-1mentioning

confidence: 99%

Amino Acid Sequence of C‐Terminal Fragment of Hog Pepsin

Kostka

Morávek

Šorm

1970

European Journal of Biochemistry

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The C-terminal fragment of hog pepsin, which had been obtained in the preceding study on the cyanogen bromide hydrolysate of this protein, was subjected to sequential studies. The 37-residue peptide was digested in independent experiments by trypsin, chymotrypsin, and pepsin, and the amino acid sequence of the arising peptides was determined. I n parallel experiments the sequence of seventeen amino acid residues in the N-terminal region of the peptide was established by the Edman degradation technique. The obtained data permit the C-terminal peptide of hog pepsin to be ascribed the amino acid sequence Asp-Val-Pro-Thr-Ser-Ser-Gly-GluLeu-Trp-Ile-Leu-Gly-Asp-Val-Phe-Ile-Arg-Gln-Tyr-Tyr-Thr-Val-Phe-Asp-Arg-Ala-Asn-Asn-LysVal-Gly-Leu-Ala-Pro-Val-Ala. These results extend and partly correct our previous knowledge of this region of the pepsin molecule as recorded in literature. The problem of the tryptophan content of pepsin is briefly discussed.

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Sulfenyl halides as modifying reagents for polypeptides and proteins. I. Modification of tryptophan residues

Cited by 219 publications

References 37 publications

Tryptophan 110, a residue involved in the toxic activity but not in the enzymatic activity of notexin

Tryptophan 110, a residue involved in the toxic activity but not in the enzymatic activity of notexin

Chemical Modification of Proteins: An Overview

Amino Acid Sequence of C‐Terminal Fragment of Hog Pepsin

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