A new zoarcid fish, Andriashevia natsushimae (Japanese name: Natsushimachojyagenge), is described on the basis of 2 specimens collected in Sagami Bay, Japan, at the depth of 850 m. This species has no pectoral fins and no pelvic fins, indicating it to be Andriashevia. It has a round body and a moderate-sized mouth in contrast to Andriashevia aptera which has a flat body and a large mouth. Phylogenic tree based on 16S ribosomal RNA (16S rRNA) sequence indicates the species had diverted at the early stage in the evolution of eelpouts.
Pyrobaculum islandicum is an ananaerobic hyperthermophilic archaeon that grows optimally at 100°C. We purified a NADH dehydrogenase from the membranes to homogeneity as analyzed by SDS-PAGE. The purified protein was suggested to comprise five subunits with molecular masses of 39 kDa, 37 kDa, 34 kDa, 31 kDa and 27 kDa, by SDS-PAGE analysis. The molecular mass of the native protein was estimated to be about 160 kDa by gel-filtration analysis. The optimal pH and temperature were 7.0 and above 80°C, respectively. The enzyme activity was shown to be highly specific to NADH, and the activity with NADPH was only 1.7% of the value with NADH.
A NADPH dehydrogenase was purified from the hyperthermophilic archaeon, Pyrobaculum islandicum. The membrane protein was solubilized by treatment with 1% Tween 20, and purified 258-fold from the cell-free extract to homogeneity as judged by SDS-PAGE analysis. The molecular mass of the enzyme was revealed to be 41 kDa both by SDS-PAGE and gel filtration analyses. The optimal pH and temperature were 7.0 and above 80°C, respectively. The Km and Vmax values were 0.69 mM and 0.25 nmol/min, respectively. It was suggested that NADPH is an electron donor in the P. islandicum electron transfer system.