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Çѱ¹»ýÅÂÇÐȸ / v.14, no.1, 1991³â, pp.101-111
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±¤Àڱؿ¡ ´ëÇÑ Amoeba ÀÇ ¹ÝÀÀ¾ç»ó°ú phosphatase ÀÇ Æ¯¼º ¹× Ȱ¼ºµµ º¯È
( The Characterization and Activity Changes of Phosphatases in Amoeba sp. to the Light Stimuli and Its Response Pattern ) |
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| Amoeba sp. was cultured under the light and the dark conditions, and the activity of phosphatases was investigated. There was a linear correlation between the early reaction time and the activity of phosphatases when phosphatases were incubated at 30¡É. Then the activity of acid phosphatase was about 2 times higher than that of alkaline phosphatase. The activity of phosphatase was optimal at pH 5.0 in acidic part and at pH 8.0 in alkaline part, respectively. The optimal temperature of phosphatases was near the 40¡É. The isozyme patterns of cytoplasmic acid phosphatase were compared with those of membraneous one. Both the isozyme patterns were shown to bo polymorphic on the polyacyamide gel, but different band patterns were observed in the isozymes of the cytoplasmic and the membraneous acid phosphatases. The number of Amoeba sp. under the light stimulus for 48 hours decreased negative exponentially from the illumination. The activity of acid and alkaline phosphatases under the illumination of light incresed 1.7 and 1.5 times higher, respectively, than the activity of those under the dark condition. This result apperars to be related to the mechanism of the autophosphorylation. |
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The Korean Journal of Ecology / v.14, no.1, 1991³â, pp.101-111
Çѱ¹»ýÅÂÇÐȸ
ISSN : 1225-0317
UCI : G100:I100-KOI(KISTI1.1003/JNL.JAKO199111919968413)
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| ³í¹® Á¦°ø : KISTI Çѱ¹°úÇбâ¼úÁ¤º¸¿¬±¸¿ø |
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