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생쥐뇌 세포질 분획의 Acid 및 Alkaline Phosphatase 의 특성 비교 연구
강창균,이영식,조기승 ( Chang Gyun Kang,Young Seek Lee,Key Seung Cho ) 생화학분자생물학회 1990 BMB Reports Vol.23 No.3
Acid and alkaline phosphatases from mouse brain cytosol fraction were separated and partially purified with 91 and 15 folds, respectively, by DEAE-cellulose column chromatography and Sephadex G-150 gel chromatography. Acid phosphatase (ACPase, EC 3.1.3.2) showed substrate specificity only to p-nitrophenylphosphate among the several substrates tried, such as, adenosine-3`-monophosphate (3`-AMP), adenosine-5`-monophosphate (5`-AMP), adenosine-5`-triphosphate (5`-ATP), glucose-6-phosphate (G-6-P), inositol-1`-monophosphate (IP), inositol-1,4,5-triphosphate (IP₃ and p-nitrophenylphosphate (PNPP). On the other hand, alkaline phosphatase (ALPase, EC 3.1.3.1) showed to active to PNPP and IP substrates among them. ACPase and ALPase showed the maximum enzyme activities at pH 5.2 with 50 mM acetate buffer and at pH 7.8 with 50 mM Hepes buffer in the presence of Mg^(2+), respectively. In the effect of Na^+ and K^+ on both ACPase and ALPase, these ions had no effect at all on ACPase, but 50 mM Na^+ and 100 mM K^+ showed maximum activation on ALPase by 3.4 times. Divalent cations,Ca^(2+) and Mg^(2+) showed no effect at all on ACPase, but 0.2 mM Mg^(2+) stimulated ALPase significantly about 5 times. On the other hand, Ca^(2+) represented competitive inhibition to Mg^(2+) effect on ALPase. Ouabain had no effect at all, but L-phenylalanine showed a minor stimulation on ALPase.
생쥐뇌 세포질 분획의 Acid 및 Alkaline Phosphatase의 특성 비교 연구
강창균,이영식,조기승,Kang, Chang-Gyun,Lee, Young-Seek,Cho, Key-Seung 생화학분자생물학회 1990 한국생화학회지 Vol.23 No.3
Acid and alkaline phosphatases from mouse brain cytosol fraction were separated and partially purified with 91 and 15 folds, respectively, by DEAE-cellulose column chromatography and Sephadex G-150 gel chromatography. Acid phosphatase (ACPase, EC 3.1.3.2) showed substrate specificity only to p-nitrophenylphosphate among the several substrates tried, such as, adenosine-3'-monophosphate (3'-AMP), adenosine-5'-monophosphate (5'-AMP), adenosine-5'-triphosphate (5'-ATP), glucose-6-phosphate (G-6-P), inositol-1'-monophosphate (IP), inositol-1,4,5-triphosphate $(IP_3)$ and p-nitrophenylphosphate (PNPP). On the other hand, alkaline phosphatase (ALPase, EC 3.1.3.1) showed to active to PNPP and IP substrates among them. ACPase and ALPase showed the maximum enzyme activities at pH 5.2 with 50 mM acetate buffer and at pH 7.8 with 50 mM Hepes buffer in the presence of $Mg^{2+}$, respectively. In the effect of $Na^+$ and $K^+$ on both ACPase and ALPase, these ions had no effect at all on ACPase, but 50 mM $Na^+$ and 100 mM $K^+$ showed maximum activation on ALPase by 3.4 times. Divalent cations, $Ca^{2+}$ and $Mg^{2+}$ showed no effect at all on ACPase, but 0.2 mM $Mg^{2+}$ stimulated ALPase significantly about 5 times. On the other hand, $Ca^{2+}$ represented competitive inhibition to $Mg^{2+}$ effect on ALPase. Ouabain had no effect at all, but L-phenylalanine showed a minor stimulation on ALPase. 생쥐 뇌 세포질 분획을 DEAE-Cellulose Chromatography와 Sephadex G-150 gel Chromatography 등에 의해 acid 및 alkaline phosphatase로 분리, 부분정제하였을 때 각각 91배와 15배의 정제율을 나타내는 분획을 얻었다. 이들의 기질특이성을 보았을 때, 사용한 여러 기질 중에서 acid phosphatase(ACPase)는 p-nitrophenylphosphate에만 작용하였으며, alkaline phosphatase(ALPase) 경우는 p-nitrophenylphosphate 외에도 inositol phosphate를 가수분해하는 특성을 나타냈다. ACPase는 50 mM acetate buffer, pH 5.2에서 최고 활성도를, ALPase 경우는 $Mg^{2+}$ 존재하의 50 mM Hepes buffer, pH 7.8에서 최고의 활성도를 나타냈다. 여러 무기이온의 영향을 보았을 때, ACPase는 $Na^+$와 $K^+$ 및 $Mg^+$ 등에 의해 전혀 영향을 받지 않았으나, ALPase 경우는 $Na^+$ 50 mM과 $K^+$ 100 mM 에서 약 3.4배의 활성화를 나타냈고, 한편 0.2mM $Mg^{2+}$에 의해서는 약 5배의 활성도 증가를 보였으며, $Ca^{2+}$에 의해서는 저해현상과 동시에 $Mg^{2+}$에 대해 경쟁적 저해를 나타냈다. ALPase에 대한 ouabain 및 L-phenylalanine의 영향을 보았을 때, ouabain은 별 영향이 없었으나, L-phenylalanine의 경우는 약간의 활성화를 나타냈다.