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翻訳と辞書　辞書検索 [ 開発暫定版 ] スポンサード リンク Secondary plot (kinetics) ： ウィキペディア英語版 Secondary plot (kinetics) In enzyme kinetics, a secondary plot uses the intercept or slope from several Lineweaver-Burk plots to find additional kinetic constants. For example, when a set of v by () curves from an enzyme with a ping–pong mechanism (varying substrate A, fixed substrate B) are plotted in a Lineweaver–Burk plot, a set of parallel lines will be produced. The following Michaelis–Menten equation relates the initial reaction rate ''v''0 to the substrate concentrations () and (): :$$ \begin \frac &= \fracA}+\fracB}+\frac \end The y-intercept of this equation is equal to the following: :$$ \begin \mbox = \fracB}+\frac \end The y-intercept is determined at several different fixed concentrations of substrate B (and varying substrate A). The y-intercept values are then plotted versus 1/() to determine the Michaelis constant for substrate B, $K\_M^B$, as shown in the Figure to the right. The slope is equal to $K\_M^B$ divided by $v\_\backslash max$ and the intercept is equal to 1 over $v\_\backslash max$. ==Secondary Plot in Inhibition Studies== A secondary plot may also be used to find a specific inhbition constant, kI. For a competitive enzyme inhibitor, the apparent Michaelis constant is equal to the following: :$$ \begin \mbox K_m=K_m\times \left(1+\frac\right) \end The slope of the Lineweaver-Burk plot is therefore equal to: :$$ \begin \mbox =\frac\times \left(1+\frac\right) \end If one creates a secondary plot consisting of the slope values from several Lineweaver-Burk plots of varying inhibitor concentration (), the competitive inhbition constant may be found. The slope of the secondary plot divided by the intercept is equal to 1/kI. This method allows one to find the kI constant, even when the Michaelis constant and vmax values are not known. 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Secondary plot (kinetics)」の詳細全文を読む スポンサード リンク 翻訳と辞書 : 翻訳のためのインターネットリソース Copyright(C) kotoba.ne.jp 1997-2016. All Rights Reserved.