北京印刷学院学报
北京印刷學院學報
북경인쇄학원학보
Journal of Beijing Institute of Graphic Communication
2009年
6期
80~82
,共null页
ATP合酶 催化模型 稳态特征
ATP閤酶 催化模型 穩態特徵
ATP합매 최화모형 은태특정
ATPase; catalysis model; steady-state character
根据实验现象，提出一个ATP合酶的三态催化模型，研究其稳态时各催化态的占有几率、速度与ATP浓度、负载力的关系，并分析各个关系的特征。结果表明，三态模型符合ATP合酶的生物学特征，定性、半定量地解释了ATP合酶的旋转催化机制。
根據實驗現象，提齣一箇ATP閤酶的三態催化模型，研究其穩態時各催化態的佔有幾率、速度與ATP濃度、負載力的關繫，併分析各箇關繫的特徵。結果錶明，三態模型符閤ATP閤酶的生物學特徵，定性、半定量地解釋瞭ATP閤酶的鏇轉催化機製。
근거실험현상，제출일개ATP합매적삼태최화모형，연구기은태시각최화태적점유궤솔、속도여ATP농도、부재력적관계，병분석각개관계적특정。결과표명，삼태모형부합ATP합매적생물학특정，정성、반정량지해석료ATP합매적선전최화궤제。
From the experimental phenomena, a three-state catalysis model is put forward. At the steady state, the occupation probability of binding-state and the rotation rate change versus ATP concentration and the load are analyzed respectively. The results indicate that the three-state catalysis model accords with the biologic characters of ATPase, and explains qualitatively and quasi-quantificationally the catalysis meehanism of ATPase.
