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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Contamination of highly purified human serum cholinesterase by dipeptidyl peptidase IV causing hydrolysis of substance P.

The purification and kinetic characterization of cholinesterase from blood plasma (pseudocholinesterase; butyrylcholinesterase: EC is described. The hydrolysis of the artificial peptide substrate Lys-Pro-p-nitroanilide served as a model of the second step in degradation of substance P by dipeptidyl peptidase IV. The substrate is hydrolyzed by a gel-electrophoretic homogeneous cholinesterase preparation with a reaction rate of 5.8 mumol/min X mg and a KM value of 0.12 mmol/l. The proteolytic reaction could not be affected with typical cholinesterase inhibitors NaF and dibucain. On the other hand Lys (pNO2-Z)-Pro and a specific suicide substrate (diacylhydroxylamine derivative) inhibit the activity in a manner analogous to dipeptidyl peptidase IV. Though these active site-directed inhibitors also influenced the benzoylcholine hydrolyzing activity of serum cholinesterase, we conclude from the data that dipeptidyl peptidase IV was the true Lys-Pro-p-nitroanilide cleaving activity. Furthermore, the conclusion can also be drawn that hydrolysis of substance P reported by Lockridge 1982 is caused by the contamination that cannot be completely separated from the esterase during the purification method used.[1]


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