Table I.
MS analysis, α-helical content, lipid transfer activity, and papain inhibition of the recombinant Gb-nsLTP1 proteins
| Strain | Experimental Mass (Theoretical)a | α-Helical Contentb | Lipid Transfer Activityc | Papain Inhibitionc |
|---|---|---|---|---|
| D | % | |||
| Wild type | 9,586.9 ± 1.2 (9,587.0) | 22 | 100 ± 7 | 100 ± 12 |
| R46A mutant | 9,502.3 ± 0.5 (9,501.9) | 21 | 88 ± 5 | 94 ± 8 |
| P79A mutant | 9,561.4 ± 0.9 (9,561.0) | 11 | 58 ± 2 | 231 ± 25 |
| F80A mutant | 9,511.6 ± 0.7 (9,510.9) | 10 | 26 ± 4 | 219 ± 2 |
| I82A mutant | 9,545.6 ± 0.8 (9,544.9) | 18 | 101 ± 1 | 97 ± 12 |
a
Including the formation of four disulfide bonds.
b
Measured at pH 7.0 and estimated by the method of Chen et al. (1972).
c
Calculated based on the lipid transfer activity or papain inhibition of the wild-type protein. These values of the native protein were 116% and 115% under the corresponding condition, respectively.