Electrophoretic analysis of cholinesterase in plasma and liver was performed with the new technique.
In the commonly used Gomori's technique for histochemical determination of cholinesterase activity, the thiocholine ester used as substrate is hydrolysed by cholinesterase, and the liberated thiocholine is captured by Cu ion as colorless copper-thiocholine precipitate, which is converted to brownish CuS by treatment with yellow ammonium sulfide.
In the present technique, silver nitrate was used instead of yellow ammonium sulfide. In this method, cholinesterase activity was demonstrable more sharply and stably.
On Cellogel electrophoresis, plasma cholinesterase (P-ChE) was separated into P-ChE
1 and P-ChE
2, which migrated with the mobility of serum α
2 and α
2-β globulins, respectively.
Liver cholinesterase (L-ChE) was separated into L-ChE
1 and L-ChE
2, which migrated with the mobility of serum α
2-β and γ globulins, respectively, by the same method.
Specific activity of L-ChE
1 was much lower than that of P-ChE
2, while, no fraction corresponding to L-ChE
2 in mobility was found in human plasma.
It was thus demonstrated that plasma cholinesterase was not identical with that of liver. Consequently, cholinesterase was not thought to be released directly into blood from liver cell without modification.
抄録全体を表示