The pineal hormone melatonin (5-methoxy-N-acetyltryptamine) has been r
eported to participate in important physiological processes. Although
some of its biological actions seem to depend on a protein receptor at
the membrane surface, melatonin is known to interact with a large var
iety of tissues and cells, suggesting that the molecule may not necess
arily interact through a specific membrane receptor at a specific cell
. Most discussions of melatonin activity have assumed that the molecul
e is highly hydrophobic. Contrary to belief, the present work shows th
at melatonin is soluble in a purely aqueous medium up to 5 x 10(-3) M
and describes a new method of melatonin preparation which shows the hi
gh hydrophilicity of the molecule. The results presented will affect t
he current biological hypothesis on the need of a melatonin carrier in
the blood stream or the mechanisms which allow the hormone to cross t
he cell membrane and interact at the level of the nucleus.