Evidence that eel acetylcholinesterase is not an integral membrane protein.
Detergent binding studies indicated that the neural enzyme, acetylcholinesterase, did not exhibit the properties of an integral membrane protein. The 11S form was isolated by affinity chromatography from a tryptic digest and the 14S and 18S forms in like manner from an undigested preparation. Studies were performed with [3H]TX-100 to determine the extent of binding by these forms and with catalase and human low density lipoprotein as reference proteins. All forms of the enzyme bound less than 0.04 mg TX-100/mg protein which is only slightly higher than binding by catalase and about 25 fold lower than the binding exhibited by low density lipoprotein.
D000110:Acetylcholinesterase / Q000032:analysis*; D000818:Animals; D002374:Catalase / Q000032:analysis; D002499:Centrifugation, Density Gradient; D002845:Chromatography; D004524:Eels; D008077:Lipoproteins, LDL / Q000032:analysis; D008565:Membrane Proteins / Q000032:analysis*; D011485:Protein Binding; D013570:Synaptic Membranes / Q000201:enzymology
D008077:Lipoproteins, LDL; D008565:Membrane Proteins; D002374:Catalase; D000110:Acetylcholinesterase