Abstract
General anæsthetics affect a number of cellular systems (e.g., cleavage figures in sea-urchin eggs, mitosis in metaphase, the beating of cilia); cytoplasmic microtubules are found in all these situations. These microtubules, which are thought to give rigidity to cytoplasm, are rings of protein units bound longitudinally; individual units can be depolymerised to subunits of molecular weight around 60,000. Several agents (cold, high hydrostatic pressure, and colchicine) can reversibly depolymerise microtubules, probably by interference with protein interactions; heavy water favours polymerisation. Cold, high pressure, or colchicine can produce narcosis, and heavy water can antagonise effects of general anæsthetics. It is suggested that microtubular proteins are also susceptible to reversible depolymerisation by anæsthetics, and that this is achieved by binding to non-polar sites on globular proteins. How this depolymerisation results in narcosis is not yet clear, but one possibility (suggested by the abundance of microtubules in neurons) is that microtubules participate in nerve-impulse transmission.
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