Table 1.
Sample | Trypsin | Specific Glu-C | Nonspecific Glu-C | |||
---|---|---|---|---|---|---|
Peptide 15–29 aa′ | + Oligonucleotide | Peptide 21–35 aa′ | + Oligonucleotide | Peptide 12–20 aa′ | + Oligonucleotide | |
TrwCR(wt) | 851.35 m/z | — | 796.3 m/z | — | 515.25 m/z | — |
‘+4' complex | — | 1480.95 m/z | 796.3 m/z | — | — | 1144.85 m/z |
‘+4+4' complex | — | — | — | — | — | 1144.85 m/z |
The results of mass spectrometry experiments are outlined in this table. The sample analyzed in each case is shown in the left column. Three different digestions were carried out with Trypsin, Glu-C using specific cleavage conditions and Glu-C using nonspecific cleavage conditions, respectively. In each case, the presence/absence of peptide or complex was analyzed. m/z values indicate that the peak corresponding to the theoretical m/z expected for that sample has been found, on the contrary, — indicates that the peak did not appear.