|
| |
|
|
|
|
||||
| Home Help Feedback Subscriptions Archive Search Table of Contents | ||||
| ||||||||||||||||||||
Files in this Data Supplement:
Fig. S1. Activity staining of a native polyacrylamide gel for heat-treated malate dehydrogenases (MDHs) of (A) Lottia digitalis and (B) L. austrodigitalis. A homogenate of foot muscle (see Materials and methods) was centrifuged at 3000 g for 1 h and the supernatant was removed and heated at different temperatures for 3 min. C, control without heat treatment; 1, 47.2°C; 2, 47.5°C; 3, 48.2°C; 4, 49.2°C; 5, 50.4°C; 6, 51.5°C; 7, 52.7°C; 8, 53.8°C; 9, 55.0°C; 10, 56.1°C; 11, 56.8°C; and 12, 57.0°C. After being heated at temperatures over 50.4°C for 3 min, the mitochondrial isoform of MDH (mMDH), which is more thermally labile than cytosolic malate dehydrogenase (cMDH), was fully denatured.
Fig. S2. Nucleotide sequences of the coding regions of cmdh cDNAs from L. digitalis (l.d., EU863452), L. austrodigitalis (l.a., EU863454), L. pelta (l.p., EU863453), L. scutum (l.scu., EU863456), L. gigantea (l.g., EU863455) and L. scabra (l.sca., EU863457). The substitutions between L. digitalis and L. austrodigitalis cDNAs are shown in red.
| ||||||||||||||||||||
