Table 1.
Modification rates for actin peptides in absence and presence of cofilin, averaged from duplicate experiments
| No. | Peptide | Protease | Oxidized residues | Subdomain | Modification rate, s−1 |
Degree of protection† | |
|---|---|---|---|---|---|---|---|
| Actin | Actin/cofilin | ||||||
| 1 | 1–18 | Trypsin | C10, L16 | 1 | 3.1 ± 0.2 | 0.7 ± 0.1 | 4.4 |
| 2 | 19–28 | F21 | 1 | 0.7 ± 0.1 | 0.8 ± 0.1 | 0.9 | |
| 3 | 40–50 | H40, M44, M47 | 2 | 12.9 ± 0.5 | 5.6 ± 0.6 | 2.3 | |
| 4 | 51–61 | Y53 | 2 | 0.9 ± 0.2 | 0 | High | |
| 5 | 63–68 | L67 | 2 | 0.4 ± 0.1 | 0.06 ± 0.03 | 6.7 | |
| 6 | 69–84 | Y69,H73,W79,M82 | 1+2 (70-) | 5.8 ± 0.6 | 2.3 ± 0.7 | 2.5 | |
| 7 | 85–95 | H87, H88, F90, Y91 | 1 | 2.7 ± 0.3 | 0.3 ± 0.1 | 9.0 | |
| 8 | 96–113 | H101, P102, L110, P112 | 1 | 1.8 ± 0.1 | 0.16 ± 0.05 | 11.3 | |
| 9 | 119–147 | M119, M123, F124, Y143 | 1+3 (145-) | 4.6 ± 0.1 | 4.0 ± 0.4 | 1.2 | |
| 10 | 148–177 | H161, P164, Y166, Y169, L171, P172, H173, M176 | 3 | 13.5 ± 0.5 | 6.3 ± 0.1 | 2.1 | |
| 11 | 184–191 | M190 | 4 | 4.4 ± 0.1 | 2.3 ± 0.2 | 1.9 | |
| 12 | 197–206 | F200-T202* | 4 | 0.7 ± 0.0 | 0 | High | |
| 13 | 239–254 | P243 | 4 | 2.5 ± 0.1 | 0.6 ± 0.1 | 4.2 | |
| 14 | 292–312 | M305-P307* | 3 | 3.7 ± 0.1 | 1.9 ± 0.4 | 1.9 | |
| 15 | 316–326 | P322, M325 | 3 | 4.9 ± 0.1 | 1.8 ± 0.0 | 2.7 | |
| 16 | 329–335 | P332, P333 | 3 | 1.5 ± 0.3 | 1.4 ± 0.2 | 1.1 | |
| 17 | 337–359 | Y337, L346, L349, F352, M355 | 1 (338-) +3 | 2.5 ± 0.3 | 3.1 ± 0.4 | 0.8 | |
| 18 | 360–372 | Y362, P367, H371 | 1 | 2.4 ± 0.2 | 0.5 ± 0.0 | 4.8 | |
| 19 | 118–125 | Glu-C | M119, M123, F124 | 1 | 2.0 ± 0.4 | 0.5 ± 0.1 | 4.0 |
| 20 | 260–270 | M269 | 4 | 2.0 ± 0.1 | 1.2 ± 0.2 | 1.7 | |
*Specific probe sites can not be determined definitely.
†Defined as ratio of modification rate of actin to actin/cofilin complex.