TABLE 2.
Peptidea | Peptide sequence and sites of cleavage by RPP and MPPb | Degradation by RPPc (%) |
---|---|---|
1 | LSALARPVGAA↓LRRS↓↑FSTSAQNNAKVA | 59 |
2 | MLAAKNILNRSSLSSS↓↑FRIATRL↓QSTKVQGSA | 39 |
3 | LSRVAKRA↓↑FSSTVANP | 20 |
4 | MLRAA↓LTTVRRGPRLSR↓L↓↑LSAAATSAVPA | 17 |
5 | MFS↓KLAHL↓Q↓RPA↓VLSRG↑VHSSVASA | 17 |
6 | MLSAARLQFAQGSVRR↓↑LTVSARDAPTKISTLA | 9.5 |
7 | GRWRLLVRPRAGAGG↓LRGSRGPGLGGGAVATRT↑LSV | 7.3 |
8 | LSLRQSIRFFKPATRT↑LCSSTYLL | <1 |
Peptide 1, mouse MDH2-28; 2, yeast heat shock protein SSC1 (amino acids 1 to 32); 3, yeast MDH2-17; 4, mouse aldehyde dehydrogenase (amino acids 1 to 29); 5, human ornithine aminotransferase (amino acids 1 to 25); 6, yeast ubiquinol cytochrome c reductase subunit 2 (amino acids 1 to 32); 7, bovine ADX18-57; 8, yeast COXIV2-25.
Arrows (↓) denote RPP cleavage sites for peptides that can be detected or MPP cleavage sites (↑).
Cleavage efficiencies are determined as described in Materials and Methods.