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사람 혈청의 Alkaline Phosphatase에 대한 Ferrous 및 Ferric 이온과 여러 계면활성제의 영향
신현수,조기승,Shin, Hyun-Soo,Cho, Key-Seung 생화학분자생물학회 1984 한국생화학회지 Vol.17 No.2
사람 혈청의 alkaline phosphatase는 glycine buffer, pH 9.8에서 최고 활성도를 보였고, 저온이나 $50^{\circ}C$의 약간 높은 온도에서도 높은 활성도를 나타냈다. 여러 양이온에 대한 효과를 보면 $Cu^{++}$ 및 $Fe^{}$ 등에 의해서만 심한 저해 효과를 나타냈을 뿐, 시험한 다른 이온들은 약간의 저해 혹은 활성 효과를 나타냈다. $Fe^{++}$이온과 $Fe^{}$이온의 영향을 비교해 본 결과 $Fe^{++}$이온에 의해서는 심한 저해 효과를 보인 반면, $Fe^{}$이온은 현저한 활성 효과를 나타냈는데, 이 결과는 혈액내에서 hemoglobin과 methemoglobin의 ferrous 및 ferric 이온에 의해 효소의 활성도가 control될 수 있을 것이라는 점을 암시해 주고 있다. 한펀 EDTA 존재하에서의 $Fe^{++}$와 $Fe^{}$이온의 영향은 preincubation조건에 따라 두 이온이 모두 활성 효과를 보였는데, EDTA 단독 존재하에서는 철저한 저해 효과를 보였다. 여러 계면활성제의 영향을 보면, 저농도의 palmitoylcarnitine, 인삼 saponin 및 TX-100 등이 현저한 효소 활성 효과를 나타냈고, SDS는 약간의 활성 효과를 SDC는 저해 효과를 보여 주었다. Alkaline phosphatase (E.C. 3.1.3.1) of human serum was shown to have a maximum activity with glycine buffer at pH 9.8 and had a still high activity even with low and a little high temperature of $50^{\circ}C$. Although the enzyme was inhibited seriously in the presence of $Cu^{++}$ and $Fe^{++}$ ions, other cations tested showed little inhibition or activation effects. In comparison of $Fe^{++}$ and $Fe^{}$ ion's effect on enzyme activity, $Fe^{++}$ ion inhibited strongly, on the other hand, the enzyme was activated meaningfully by the addition of $Fe^{}$ ion. This result suggested the possibility that ferrous and ferric ions in hemoglobin and methemoglobin, respectively, could control this enzyme activity in the blood stream. In the presence of EDTA, the enzyme activity was elevated significantly with both of $Fe^{++}$ and $Fe^{}$ ions by the change of preincubation conditions, but EDTA itself had a property to inhibit completely the activity. Among several detergents tested, low concentration of palmitoylcarnitine, ginseng saponin and triton X-100 stimulated significantly the enzyme activity in the experimental conditions used, but the inhibition was shown in high concentration of above detergents and sodium deoxycholate.
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사람 혈청의 Alkaline Phosphatase 에 대한 Ferrous 및 Ferric 이온과 여러 계면활성제의 영향
신현수,조기승 ( Hyun Soo Shin,Key Seung Cho ) 생화학분자생물학회 1984 BMB Reports Vol.17 No.2
Alkaline phosphatase (E.C. 3.1.3.1) of human serum was shown to have a maximum activity with glycine buffer at pH 9. 8 and had a still high activity even with low and a little high temperature of 50℃. Although the enzyme was inhibited seriously in the presence of Cu^(++) and Fe^(++) ions, other cations tested showed little inhibition or activation effects. In comparison of Fe^(++) and Fe^(+++) ion`s effect on enzyme activity, Fe^(++) ion inhibited strongly, on the other hand, the enzyme was activated meaningfully by the addition of Fe^(+++) ion. This result suggested the possibility that ferrous and ferric ions in hemoglobin and methemoglobin, respectively, could control this enzyme activity in the blood stream. In the presence of EDTA, the enzyme activity was elevated significantly with both of Fe^(++) and Fe^(++) ions by the change of preincubation conditions, but EDTA itself had a property to inhibit completely the activity. Among several detergents tested, low concentration of palmitoylcarnitine, ginseng saponin and triton X-100 stimulated significantly the enzyme activity in the experimental conditions used, but the inhibition was shown in high concentration of above detergents and sodium deoxycholate.
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Ferric ion($Fe^{3+}$)에 의한 사람 혈청 Acid Phosphatase의 활성화
이종호,신현수,조기승,Lee, Jong-Ho,Shin, Hyun-Soo,Cho, Key-Seung 생화학분자생물학회 1985 한국생화학회지 Vol.18 No.2
사람혈청의 Acid phosphatase(EC 3.1.3.2.)는 0.1 M acetate buffer, pH 5.0에서 최고 활성도를 나타냈다. 이 효소의 온도 영향을 보면, $0^{\circ}C$에서도 상당한 활성도를 보였고, $10^{\circ}C$까지는 약간 감소하나 온도증가에 따라 $50^{\circ}C$까지 계속 상승함을 보여 줌으로서 고온에서도 상당히 안정함을 나타냈다. 여러 금속 ion에 대한 영향을 보면, $Na^+$, $K^+$, $Ca^{2+}$, $Mg^{2+}$, $Hg^{2+}$ 및 $Cd^{2+}$ 등에 의해서는 별로 영향을 받지 않으나, $Cu^{2+}$ 와 $Fe^{2+}$에 의해서는 심한 저해 현상을 보였다. 한편 배양액에 $Fe^{3+}$를 가했을 때 ACPase는 대조구보다 2.5배 이상 활성화됨을 보였는데, EDTA와의 여러 반응 조건에 따라 보여준 결과는 매우 중요한 의마를 냐타내 주었다. EDTA는 ACPase에 전혀 영향을 끼치지 않았으며, $Cu^{2+}$ 와 $Fe^{2+}$의 저해 효과에 대한 EDTA의 영향을 보면, $Cu^{2+}$에 의한 효소저해는 재생시키지 않았으나 $Fe^{2+}$에 의한 저해는 60%정도 재생시킴으로서 $Cu^{2+}$이 효소의 활성부위와 견고하게 binding됨을 알 수 있게 하였다. Ferric ion($Fe^{3+}$)의 ACPase 활성화에 있어서, EDTA를 $Fe^{3+}$과 1분간 preincubation시켰을때 3.5배 이상 효소활성도를 촉진시켰으며, 효소를 $Fe^{3+}$과 1분간 preincubation시킨후 EDTA를 가했을때는 이보다 약간 감소되는 결과를 보였으나, 효소활성을 대조구보다 상당히 활성화시킴을 나타냈다. The acid phosphatase (EC 3.1.3.2.) of human serum has shown to have a maximum activity with 0.1 M acetate buffer at pH 5.0 and had an appreciable activity at a low of $0^{\circ}C$ and also a stable character even with a little high temperature of $50^{\circ}C$ Among several heavy metal ions tested, $Na^+$, $K^+$, $Ca^{2+}$, $Mg^{2+}$, $Hg^{2+}$ and $Cd^{2+}$ did not affected significantly, but $Cu^{2+}$ and $Fe^{2+}$ inhibited enzyme activity seriously. On the other hand, addition of $Fe^{3+}$ to incubation mixture, it stimulated the acid phsophatase more than 2.5 times. EDTA had no effect on the enzyme at all, and rather restored some extent of the inhibitory effect by $Fe^{2+}$ From this result, affinity of $Cu^{2+}$ to enzyme active site was stronger than that of $Fe^{2+}$. In the case of $Fe^{3+}$ stimulation, the enzyme activity was increased more than 3.5 times when $Fe^{3+}$ was preincubated with EDTA for 1 min before addition of enzyme and substrate. And also preincubation of enzyme with $Fe^{3+}$ before addition of EDTA and substrate, it showed a little reduced activity but still high stimulation when it compared with control group.
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Ferric ion ( Fe3+ ) 에 의한 사람혈청 Acid Phopshatase 의 활성화
이종호,신현수,조기승 ( Jong Ho Lee,Hyun Soo Shin,Key Seung Cho ) 생화학분자생물학회 1985 BMB Reports Vol.18 No.2
The acid phosphatase (EC 3.1.3.2.) of human serum has shown to have a maximum activity with 0.1 M acetate buffer at pH 5.0 and had an appreciable activity at a low of 0℃ and also a stable character even with a little high temperature of 50℃. Among several heavy metal ions tested, Na^+, K^+, Ca^(2+), Hg^(2+) and Cd^(2+) did not affected significantly, but Cu^(2+) and Fe^(2+) inhibited enzyme activity seriously. On the other hand, addition of Fe^(3+) to incubation mixture, it stimulated the acid phsophatase more than 2.5 times. EDTA had no effect on the enzyme at all, and rather restored some extent of the inhibitory effect by Fe^(2+). From this result, affinity of Cu^(2+) to enzyme active site was stronger than that of Fe^(2+). In the case of Fe^(3+) stimulation, the enzyme activity was increased more than 3.5 times when Fe^(3+) was preincubated with EDTA for 1 min before addition of enzyme and substrate. And also preincubation of enzyme with Fe^(3+) before addition of EDTA and substrate, it showed a little reduced activity but still high stimulation when it compared with control group.
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