Optimization by mass spectrometry of a tryptophan-specific protein cleavage reaction.
Mass spectrometry has been used to define the reaction of BNPS-skatole (3-bromo-3-methyl-2-(o-nitrophenylsulfenyl)indolenine) with selected proteins and peptides, confirming the cleavage of the protein chain at tryptophan residues, characterizing the products, and identifying the side reactions. A short procedure for carrying out the cleavage reaction with minimal side reactions is presented.
Vestling
M M
MM
Department of Chemistry and Biochemistry, University of Maryland Baltimore County, Baltimore.
Kelly
M A
MA
Fenselau
C
C
D000478:Alkylation; D000595:Amino Acid Sequence; D000803:Angiotensin I / Q000737:chemistry; D000818:Animals; D006736:Horses; D007202:Indicators and Reagents; D013058:Mass Spectrometry; D008555:Melitten / Q000737:chemistry; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D011506:Proteins / Q000737:chemistry*; D012862:Skatole / Q000031:analogs & derivatives; D013004:Somatostatin / Q000737:chemistry; D053561:Somatostatin-28; D014305:Triose-Phosphate Isomerase / Q000737:chemistry; D014364:Tryptophan / Q000737:chemistry*
D007202:Indicators and Reagents; D011506:Proteins; D008555:Melitten; C005904:BNPS-skatole; D013004:Somatostatin; D053561:Somatostatin-28; D014364:Tryptophan; D000803:Angiotensin I; D012862:Skatole; D014305:Triose-Phosphate Isomerase