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Detection and Characterization of Extracellular Phospholipase $A_2$ Activity in Human Amniotic Fluid
백석환,이승호,장현욱,Baek, Suk-Hwan,Lee, Seung-Ho,Chang, Hyeun-Wook 생화학분자생물학회 1992 한국생화학회지 Vol.25 No.3
사람의 양수 중에서 처음으로 세포외성 phospholipase $A_2$ 활성이 있음을 확언하였으며, 출산에 있어서 중요한 prostaglandin의 전구체인 arachidonic acid 제공에 중요한 역활을 할 것이라고 생각된다. 본 효소는 지금까지 보고된 group I이나 group II phospholipase $A_2$와 계변 활성제의 영향이나 monoclonal antibody와의 반응성에서 다른 특성을 갖는 효소로 추정되었으며, 또한 적어도 2종류의 phospholipase $A_2$의 활성이 존재함에 시사되어 금후 더욱 구체적인 검토를 행하여 단백화학적 특성을 규명할 필요가 있다. Extracellular phospholipase $A_2$ activity has been identified in human amniotic fluid. This enzyme required $Ca^{2+}$ ion and exhibited bimodal pH optimum at pH 7.0 and 9.0. The phospholipase hydrolyzed 1-acyl-2-[1-$^{14}C$]arachidonoylphosphatidylethanolamine to form only [$^{14}C$]arachidonic acid indicating that the enzyme had phospholipase "$A_2$" activity. Ionic and non-ionic detergents caused loss of enzymatic activity. This phospholipase $A_2$ was recognized, in part, by a monoclonal antibody raised against phospholipase $A_2$ from human synovial fluid. This finding suggests that our enzyme is an another type of an extracellular phospholipase $A_2$ which may not belong to the 14 KDa group II phospholipase $A_2$ family.
사람 양수 중의 세포외성 Phospholipase A2 특성
백석환,이승호,장현욱 ( Suk Hwan Baek,Seung Ho Lee,Hyeun Wook Chang ) 생화학분자생물학회 1992 BMB Reports Vol.25 No.3
Extracellular phospholipase A₂ activity has been identified in human amniotic fluid. This enzyme required Ca^(2+) ion and exhibited bimodal pH optimum at pH 7.0 and 9.0. The phospholipase hydrolyzed 1-acyl-2-[1-^(14)C]arachidonoylphosphatidylethanolamine to form only [^(14)C]arachidonic acid indicating that the enzyme had phospholipase $quot;A₂$quot; activity. Ionic and non-ionic detergents caused loss of enzymatic activity. This phospholipase A₂ was recognized, in part, by a monoclonal antibody raised against phospholipase A₂ from human synovial fluid. This finding suggests that our enzyme is an another type of an extracellular phospholipase A₂ which may not belong to the 14 KDa group II phospholipase A₂ family. v
백석환,다까야마기요시,구도이찌로,이노우에게이조,이현우,도준영,장현욱 영남대학교 약품개발연구소 1992 영남대학교 약품개발연구소 연구업적집 Vol.2 No.-
Extracellular phospholipase A₂ activity has been identified in pleural fluid of patients with tuberculosis. This enzyme is a calcium requiring protein and has a pH optimum of 10.0. The enzyme was inhibited by the active site-directed histidine reagent, p-bromophenacyl bromide, lonic and non-ionic detergents, or the sulfhydryl reagent dithiothreitol, caused loss of enzyme activity. When substrate specificity was tested using 2-[1-^(l4)C]linoleoyl phospholipids as substrates, phosphatidyl-ethanolamine was the best substrate, followed by phosphatidylserine and phosphatidylcholine. This phospholipase A₂ showed high affinity for heparin, and was recognized by a monoclonal antibody raised against phospholipase A₂ from human synovial fluid. These findings suggest that an extracellular phospholipase A₂, which may belong to the 14K group Ⅱ phospholipase A₂ family, exists in the pleural fluid of patients with tuberculosis.