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성견악하선에서 Na+, K+ - activated Adenosine Triphosphatase에 대한 실험적 연구

Other Titles
 (An) experimental study on Na+, K+ - activated adenosine triphosphatase in dog submaxillary gland 
Issue Date
1985
Description
치의학과/석사
Abstract
[한글]저자는 성견의 악하선에서 Na**+, K**+ -ATPase를 균등짙액, 과립체 분뵉, 블연속성 당 밀도등급도 및 연속성 당 밀도 등급도 순으로 순수 정제 분리를 시도하여 다음과 같은 성적을 얻었다. 1. 균등질액내 Na**+, K**+ -ATPase의 Specific activity는 0.63μmoles/min/mg·protein이었다. 2. 과립체 분획내 Ma**+, K**+ -ATPase의 specific activity는 2.79μmoles/min/mg·protein으로 균등질액에서 보다 4,4배 분리 정제되었으며 80% 효소 최수율을 나타내었다. 3. 불연속성 당 밀도 등급도내의 Na**+, K**+ -ATPase의 specific activity는 20.41μmoles/min/mg·protein으로 균등질액에서 보다 32.4배 분리 정제되었으며 20% 효소 회수율을 나타내었다. 4. 연속성 당 밀도 등급도내의 Na**+, K**+ -ATPase의 specific activity는 분획 11에서 가장 높게 나타났으며 , 그 때의 밀도는 .1.10-1.12g/ml이었고 specific activity는 36.29μmoles/min/mg·protein으로 균등질액에서 보다 57.6배 분리 정제되었다.
[영문]Experimental study of purificating trials and specific activity of Na**+, K**+, -activity Adenosine Triphosphatase in dog submaxillary gland was done and results were obtained as follow ; 1. In homogenate, the specific activity of Na**+, K**+ -ATPase was 0.63μmoles/min/mg-protein. 2. In microsomal fraction, the specific activity of Na**+, K**+ -ATPase was 2.79μoles/min/mg·trotein. The enzyme was purified 4.4-fold than in homogenate and recovery rate was 80%. 3. In discontinuous gradient, the specific activity of Na**+. K**+ -ATPase was 20.41μmoles/min/mg·protein. The enzyme was purified 32.4-fold than in homogenate and recovery rate was 20%. 4. In linear gradient, the specific activity if Na**+, K**+-ATPase was the highest at fraction 11, and the density was 1.10∼1.12g/ml at that, The specific activity was 36.29μmoles/min/mg·protein, and the enzyme was purified 57.6-fold than in homogenate.
URI
http://ir.ymlib.yonsei.ac.kr/handle/22282913/115567
Appears in Collections:
2. 학위논문 > 2. College of Dentistry (치과대학) > 석사
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