Biological Role of Cl-esterase

概要

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The purification procedure of Cl-esterase and Cls from human plasma was described, and some properties of these enzymes were characterized. Cl-esterase was purified from euglobulin of human plasma by successive column chromatography with DEAE-cellulose, hydroxylapatite and TEAE-cellulose. The final product was found to be homogeneous upon ultracentrifugal and disc-electrophoretic analysis. The S20, w was 4.3 and the molecular weight was determined as 113, 000 by gel filtration using Sephadex G-200. Purified Cl-esterase released kinin from human plasma kininogen I and II. This enzyme did not activate purified plasminogen or plasma kallikreinogen. Cls, proenzyme of Cl-esterase, was purified from euglobulin fraction of human plasma by DEAE-cellulose and hydroxylapatite column chromatography. The final product was found to be homogeneous upon ultracentrifugal, disc-electrophoretic and immunoelectrophoretic analysis. The S20, w was 8.4 and the molecular weight was determined as 180, 000. No conversion of Cls into Cl-esterase was observed upon incubation of purified Cls alone or addition of purified Cl-esterase. However, the addition of Clr or trypsin caused a rapid conversion of Cls into Cl-esterase. Moreover, it was found that purified plasmin and plasma kallikrein converted Cls into Cl-esterase at a very slow rate.
Japan Society of Clinical Chemistryの論文