Distribution and solubilization of the molecular forms of acetylcholinesterase in rat urinary bladder and sphincter.
The distribution and solubility of the molecular forms of acetylcholinesterase (acetylcholine acetylhydrolase, EC 3.1.1.7) were examined in adult, male rat bladder body and sphincter. Four distinct forms of the enzyme solubilized from bladder body were separated on sucrose density gradients. Two of the forms (A8 and A12) corresponded to asymmetric proteins and were solubilized with high ionic strength buffer. The other two forms represented globular forms. The smallest form (G1) was soluble in low ionic strength buffer without detergent. About 33% of the larger globular form (G4) required detergent for solubilization. There were only minor differences in the distribution of these forms in juvenile rat bladder and adult, female rat bladders. Sphincter tissue lacked one of the asymmetric forms but otherwise resembled the bladder bodies. These results demonstrate that some smooth muscle organs have significant amounts of asymmetric, as well as globular, forms of acetylcholinesterase and suggest that additional studies should be performed to characterize the enzyme in this and other smooth muscle systems.
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Division of Pharmacology and Medicinal Chemistry, College of Pharmacy, University of Cincinnati, OH 45267-0004.
D000110:Acetylcholinesterase / Q000032:analysis*; D001003:Anal Canal / Q000201:enzymology*; D000818:Animals; D002499:Centrifugation, Density Gradient; D005260:Female; D046911:Macromolecular Substances; D008297:Male; D009994:Osmolar Concentration; D051381:Rats; D012995:Solubility; D014018:Tissue Distribution; D001743:Urinary Bladder / Q000201:enzymology*
D046911:Macromolecular Substances; D000110:Acetylcholinesterase