1 Double reciprocal analysis of initial velocities of AcpS
2 substrate concentration data were plotted in
double-reciprocal form, all line patterns were intersect
3 Double-reciprocal patterns of velocity versus substrate
4 reated control eyes fit a straight line on a
double reciprocal plot (r2 = 0.98) after the introductio
5 d-end inhibitor for GGPP, gave a competitive
double reciprocal plot for varied concentrations of GGPP
6 ndary to AMD Study), which were plotted on a
double reciprocal plot of 1 / lesion size (disc area) vs
7 From a
double-reciprocal plot of k(obs) versus [H(2)O(2)] at pH
8 Double reciprocal plots and preincubation studies reveal
9 Double reciprocal plots for coenzyme binding to DGD exhi
10 Double reciprocal plots for the peptide mimic Cys-AMBA-L
11 Double reciprocal plots of initial rates versus concentr
12 In this mechanism,
double reciprocal plots will appear nearly parallel (as
13 Double reciprocal plots with N-methyl-L-tryptophan as th
14 lar to MAO A, including biphasic kinetics in
double reciprocal plots.
15 Curvature is observed in the
double-reciprocal plots for product inhibition by NADH a
16 Double-reciprocal plots for two-substrate kinetic data y
17 Double-reciprocal plots of initial velocities versus the
18 Double-reciprocal plots showed a competitive inhibition
19 Although the
double-reciprocal plots with UTP produced parallel lines
20 The linearity of primary
double-reciprocal plots, in the presence and absence of
21 eine (AdoHcy) were obtained and evaluated as
double-reciprocal plots.
22 se and phosphatase both yielded intersecting
double-reciprocal plots.
23 Steady-state rate studies yield parallel
double-reciprocal plots; however, we show that fluoride
24 These results were compared with
double-reciprocal velocity plots and product analyses ob
25 sferase) and suggest a predictive ability of
double-reciprocal velocity plots for single versus multi
26 Double-reciprocal velocity plots under catalytic conditi