First all, I would like to thank those who answered my question
about cnbr/KI cleavage in trp. Now I am reporting that I have successful
cleavage in high yield (65%) overnight reaction room temperature (25C) in
70% TFA compared to obtaneid by BNPS-SK which yielded 30% after 96h at 37C
in 80% acetic acid. The great point was that I have obtained a superclean
chromatogram on the RP-HPLC which gave me two nice short peptides from the
rest of big piece of protein. But one of them is blocked and I need to use
MALDI-TOF in combination of Cp Y digestion.
1) Do someone know about the structure of trp after cleavage?
2) Do someone know if the Cp Y is going to release the first
modif trp at the C-terminal of blocked peptide?
ESI-MS would solve this problem, but I dont have one available at
moment. Thanks in advance for any input from the greatest scientific
group in the world.
Jose Cesar Rosa, M Sc
Centro de Quimica de Proteinas
Faculdade de Medicina Ribeirao Preto
Universidade de Sao Paulo
Av. Bandeirantes, 3900
14049-900 Ribeirao Preto, Brazil
phone: 55-16-6331884
fax: 55-16-6332119
cell: 55-16-9948642
email: jcrosa@fmrp.usp.br