Enzyme Kinetics Module 解析手法

基質なし	pH 依存性（6種）、初速度、熱変性、変性剤変性、指数減衰（4種）、直線
基質1個	基質１（6種）、基質１ - 阻害剤１（8種）、基質1 - 強結合阻害剤（4種）、酵素活性剤あり（Nonessential・SA Complex ）
基質2個	基質2（3種）

１　組み込まれている各基質数での実験のタイプと式およびグラフの種類

関連：Enzyme Kinetics Module の操作方法

■ 基質の数 = None

pH Rate Profile
- Equations
  - Single pKa (Rising)
    V_maxlim/(1+10^(pK_a-pH))
  - Single pKa (Falling)
    V_maxlim/(1+10^(pH-pK_a))
  - Single pKa With Offset
    (V_lim1 +V_lim2*10^(pH-pK_a))/(1+10^(pH-pK_a))
  - Bell Shaped
    (V_maxlim/(1+10^(pK_a-pH) + 10^(pH-pK_b))
  - Bell Shaped With Plateau
    V_maxlim*alpha+10^(pK_b-pH))/1+ 10^(pK_a+pK_b-2*pH)+10^(pK_b-pH)+10^(pH-pK_c))
  - Plateau Shaped
    (V_maxpla+V_maxlim*10^(pH-pK_b))/1+ 10^(pK_a-pH)+10^(pH-pK_b))
- Graphs
  - y vs. pH
  - log(y) vs.pH
  - Residual Graphs
First Order Rate
- Equations
  - First
    limit*(1-exp(-k*t))
  - First + Offset
    limit*(1-exp(-k*t))
- Graphs
  - v vs.t
  - Residual Graphs
Protein Denaturant Melt
- Equations
  - Denaturant Melt
    ff*(ub-lb)+lb
- Graphs
  - y vs. [Denaturant]
  - Residual Graphs
Protein Temperature Melt
- Equations
  - Temperature Melt
    ff*(lb-rb)+rb
- Graphs
  - y (response) vs. Temperature
  - Residual Graphs
Exponential Decay
- Equations
  - Single Exponential
    y_max*exp(-k*t)
  - Single Exponential + Offset
    y₀+y_max*exp(-k*t)
  - Double Exponential
    y_max1*exp(-k₁*t)+y_max2*exp(-k₂*t)
  - Double Exponential + Offset
    y₀+y_max1*exp(-k₁*t)+y_max2*exp(-k₂*t)
- Graphs
  - y(residuals) vs. time
  - log(y) vs. t
  - Residual Graphs
Regression
- Equations
  - Linear
    y₀+a*x
- Graphs
  - y vs. x
  - Residual Graphs

■ 基質数 = 1

Single Substrate
- Equations
  - Michaelis-Menten
    v = V_max*S/(K_m+S)
  - Substrate Inhibition (Uncompetitive)
    y= V_max/(1+K_m/S+S/K_i)
  - Substrate Activation (Ordered)
    v = V_max*(S/K_s)^2/alpha/(1+S/K_s+(S/K_s)^2/alpha)
  - Substrate Activation (Random)
    v = V_max*(S/K_s)^2/alpha/(1+S/K_s+S/(K_s/alpha)+(S/K_s)^2/alpha)
  - Hill
    v = V_max*Sⁿ/(K_mⁿ+Sⁿ)
  - Isoenzyme
    v = V_max1*(S/K_m1)/(1+S/K_m1)+V_max2*(S/K_m2)/(1+S/K_m2)
- Graphs
  - Michaelis-Menten
  - Lineweaver-Burk
  - Eadie-Hofstee
  - Scatchard
  - Hanes-Woolf
  - Hill
  - Residual Graphs
Single Substrate - Single Inhibitor
- Equations
  - Competitive (Full)
    v = V_max/(1+(K_m/S)*(1+I/K_i))
  - Competitive (Partial)
    v = V_max/(1+(K_m/S)*(1+I/K_i1)/(1+I/K_i2))
  - Noncompetitive (Full)
    v = V_max/((1+I/K_i)*(1+K_m/S))
  - Noncompetitive (Partial)
    v = V_max/((1+K_m/S)*(1+I/K_i)/(1+I*beta/K_i))
  - Mixed (Full)
    v = V_max/((K_m/S)*(1+I/K_i)+(1+I/(alpha*K_i)))
  - Mixed (Partial)
    v = V_max*((1+beta*I/(alpha*K_i))/(1+I/(alpha*K_i)))/ (1+(K_m/S)*(1+I/K_i)/(1+I/(alpha*K_i)))
  - Uncompetitive (Full)
    v = V_max/(1+I/K_i+K_m/S)
  - Uncompetitive (Partial)
    v = V_max*(1+beta*(I/K_i))/(1+I/K_i+K_m/S)
- Graphs
  - Michaelis-Menten
  - Lineweaver-Burk
  - Eadie-Hofstee
  - Scatchard
  - Hanes-Woolf
  - Hill
  - Dixon
  - Residual Graphs
Tight Binding Inhibitor
- Equations
  - Competitive Tight
    - v₀ = V_max/(K_m/S+1)
    - K_ap = K_i*((S/K_m)+1)
    - v = (v₀/(2*E))*(E-I-K_ap+sqrt((E-I-K_ap)2+4*E*K_ap))
  - Noncompetitive Tight
    - v₀ = V_max/(K_m/S+1)
    - v = (v₀/(2*E))*(E-I-K_i+sqrt((E-I-K_i)2+4*E*K_i))
  - Uncompetitive Tight
    - v₀ = V_max/(K_m/S+1)
    - K_ap = K_i*((K_m/S)+1)
    - v = (v₀/(2*E))*(E-I-K_ap+sqrt((E-I-K_ap)2+4*E*K_ap))
  - Mixed Tight
    - E = 27
    - alpha = 5.6
    - v₀ = V_max/(K_m/S+1)
    - I_ap = K_i*((S/K_m)+1)*alpha/(alpha+S/K_m)
    - v = ((v₀-v_inf)/(2*E))*(((v₀+v_inf)/(v₀-v_inf))*E-I-I_ap+sqrt((E-I-I_ap)2+4*E*I_ap))
- Graphs
  - Michaelis-Menten
  - Lineweaver-Burk
  - Eadie-Hofstee
  - Scatchard
  - Hanes-Woolf
  - Hill
  - Dixon
  - Residual Graphs
Enzyme Activator - Nonessential
- Equations
  - Nonessential
    v = V_max*(1+beta*A/(alpha*K_a))/((K_m/S)*(1+A/K_a)+(1+A/(alpha*K_a)))
- Graphs
  - Michaelis-Menten
  - Lineweaver-Burk
  - Eadie-Hofstee
  - Scatchard
  - Hanes-Woolf
  - Hill
  - Residual Graphs
Enzyme Activator - SA Complex
- Equations
  - Specific
    v = V_max*S/K_m/(1+S/K_m+K_a/A)
  - Catalytic
    v = V_max*S/K_m/(1+K_a/A+S/K_m*(1+K_a/A))
  - Mixed
    v = V_max*S/K_m/(1+K_as/A+S/K_m*(1+K_ac/A))
- Graphs
  - Michaelis-Menten
  - Lineweaver-Burk
  - Eadie-Hofstee
  - Scatchard
  - Hanes-Woolf
  - Hill
  - Residual Graphs

■ 基質数 = 2

Two Substrate
- Equations
  - Random Bi-Bi (Sequential)
    y = V_max*A*B/(alpha*K_a*K_b+K_b*A+K_a*B)+A*B)
  - Ordered Bi-Bi (Sequential)
    y = V_max*A*B/(K_a*K_b+K_b*A+A*B)
  - Ping Pong Bi-Bi (Nonsequential)
    if ((A=0)(B=0), 0, y = V_max*A*B/(K_b*A+K_a*B+A*B))
- Graphs
  - Michaelis-Menten A
  - Michaelis-Menten B
  - Lineweaver-Burk A
  - Lineweaver-Burk B
  - Eadie-Hofstee A
  - Eadie-Hofstee B
  - Scatchard A
  - Scatchard B
  - Hanes-Woolf A
  - Hanes-Woolf B
  - Hill A
  - Hill B
  - Residual Graphs

２　ユーザー定義式の登録

以下の実験タイプには式を追加することが出来ます。
- pH Rate Profile
- First Order Rate
- Protein Denaturant Melt
- Protein Temperature Melt
- Exponential Decay
- Regression

※ 酵素反応速度分析モジュール (Enzyme Kinetics Module) は、SigmaPlot 12 に標準装備されています。

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Enzyme Kinetics Module 解析手法

１ 組み込まれている各基質数での実験のタイプと式およびグラフの種類

２ ユーザー定義式の登録

１　組み込まれている各基質数での実験のタイプと式およびグラフの種類

２　ユーザー定義式の登録