May 13, 1976

Purification and characterization of butyrylcholine-hydrolyzing enzyme from Pseudomonas polycolor

Biochimica Et Biophysica Acta
T Nagasawa OgataK

Abstract

A butyrylcholine-hydrolyzing enzyme (EC 3.1.1.-) fo Pseudomonas polycolor IFO 3918 was purified approximately 9270-fold with a recovery of 9.9% by use of chromatographic techniques. The enzyme preparation appeared to be homogeneous when subjected to electrophoretic and ultracentrifugational analyses. The molecular weight was determined as approximately 59000 by gel filtration. Isoelectric focusing electrophoresis revealed that the enzyme had an isoelectric point around pH 5.1. The enzyme catalyzed the hydrolysis of butyrylcholine with the miximum activity among various esters tested, and split benzoylcholine, propionylcholine and some aliphatic esters, but did not attact acetylcholine. The estimated value of Km at pH 7.5 and 25 degrees C was 7-10(-4) M for butyrylcholine. The enzyme was irreversibly inhibited by organophosphorus compounds and carbamates, such as diisopropylphosphofluoridate and eserine. The enzyme was inhibited by some compounds, such as atropine and quinidine. Auaternary ammonium salts showed an inhibitory effect on the enzyme resembling co-operative inhibition.

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Citations

Mentioned in this Paper

Ammonium salts
Quinidex
Carbamates
Structure-Activity Relationship
Isoflurophate
Atropine
Atropinum, atropine
Butyrylthiocholinesterase
Metals
Carbamate anxiolytics

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