Title : Use of N-chlorosuccinimide/urea for the selective cleavage of tryptophanyl peptide bonds in proteins. Cytochrome c.

Pub. Date : 1977 Jul 25

PMID : 194900






4 Functional Relationships(s)
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Protein Name
Organism
1 The conditions and utility of the N-chlorosuccinimide/urea (NCS/urea) reagent for the selective cleavage of tryptophanyl peptide bonds in proteins is demonstrated with cytochrome c. N-chlorosuccinimide cytochrome c, somatic Equus caballus
2 The conditions and utility of the N-chlorosuccinimide/urea (NCS/urea) reagent for the selective cleavage of tryptophanyl peptide bonds in proteins is demonstrated with cytochrome c. N-chlorosuccinimide cytochrome c, somatic Equus caballus
3 At low concentrations of NCS/urea the oxidation of thioether side chains in cytochrome c is the predominant reaction. N-chlorosuccinimide cytochrome c, somatic Equus caballus
4 At 10-fold excess of NCS/urea reagent, cleavage of the tryptophanyl peptide bond is optimal at approximately 50% yield in several species of cytochrome c studied. N-chlorosuccinimide cytochrome c, somatic Equus caballus