Purification and functional reconstitution of the voltage-sensitive sodium channel from rabbit T-tubular membranes.
The voltage-sensitive sodium channel has been purified from rabbit T-tubular membranes
and reconstituted into defined phospholipid vesicles. Membranes enriched in T-tubular
elements (specific [3H] nitrendipine binding= 41+/-9 pmol/mg of protein, n= 7) were isolated
from fast skeletal muscle. After solubilization with Nonidet P-40, the sodium channel protein
was purified to greater than 95% of theoretical homogeneity based on the specific activity of
[3H] saxitoxin binding. Two subunits of Mr approximately 260,000 and 38,000 were found; …
and reconstituted into defined phospholipid vesicles. Membranes enriched in T-tubular
elements (specific [3H] nitrendipine binding= 41+/-9 pmol/mg of protein, n= 7) were isolated
from fast skeletal muscle. After solubilization with Nonidet P-40, the sodium channel protein
was purified to greater than 95% of theoretical homogeneity based on the specific activity of
[3H] saxitoxin binding. Two subunits of Mr approximately 260,000 and 38,000 were found; …