Reconstitution of 5-hydroxytryptamine transport from cholate-disrupted platelet plasma membrane vesicles.

The bile acid cholate disrupts platelet plasma membrane vesicles and inactivates 5-hydroxytryptamine transport activity. The transporter appears not to be solubilized by this procedure, but remains associated with a high molecular weight aggregate. Merely removing cholate does not restore the vesicular structure or transport activity, but in the presence of added soybean phospholipids, cholate removal generates proteoliposomes which accumulate 5-hydroxytryptamine. This reconstituted transport activity is similar in its ionic requirements and inhibitor sensitivity to transport in native membrane vesicles and intact platelets.