사람 혈액계 Acid Phosphatase 의 특성 비교연구 = The comparative Studies of Characteristics of Acid Phosphatas in Human blood System

다국어 초록 (Multilingual Abstract)

Acid phosphatase (ACPase)(EC 3.1.3.2) in human blood system, that is, serum, erythrocytes and erythrocyte membrane, has shown a maximum enzyme activity with 0.1 M acetate buffer at pH 5.0. ACPase showed an appreciable activity even at a low temperature of 0℃. Serum ACPase showed a stable character and a maximum activity at a high temperature of 60℃ and decreased sharply at 70℃. On the other hand, ACPases from erythrocytes and erythrocyte membrane showed maximum activities between 40℃-45℃ and decreased their activities significantly after 45℃. The time course of enzyme activity revealed the linear proportionality until 120 minutes with p-nitrophenyl phosphate as a substrate which meant no feedback inhibition occurred by the products. The result of proportional increase of ACPase by increasing amounts of erythrocytes represented that this enzyme is resided on the surface of erythrocytes. In the comparison of specific activities of ACPases from different sources, erythrocyte membrane ACPase showed enzyme activity by 95 times and erythrocyte ACPase, 15 times when they are compared with that of serum ACPase. In the effects of ferrous and ferric ions on ACPases from different sources, erythrocyte and erythrocyte membrane enzymes were inhibited by both cations, and also ferrous ion inhibited serum ACPase. But ferric ion activated the serum ACPase significantly.