biexponential kinetics
Recently Published Documents


TOTAL DOCUMENTS

4
(FIVE YEARS 0)

H-INDEX

3
(FIVE YEARS 0)

Molecules ◽  
2020 ◽  
Vol 25 (21) ◽  
pp. 5080
Author(s):  
Sergey Cherkasov ◽  
Dmitriy Parkhomenko ◽  
Alexander Genaev ◽  
Georgii Salnikov ◽  
Mariya Edeleva ◽  
...  

Three alkoxyamines based on imidazoline radicals with a pyridine functional group—potential initiators of nitroxide-mediated, controlled radical polymerization—were synthesized. Electron Paramagnetic Resonance (EPR) measurements reveal biexponential kinetics for the thermolysis for diastereomeric alkoxyamines and monoexponential kinetics for an achiral alkoxyamine. For comparison, the thermolysis of all three alkoxyamines was studied by NMR in the presence of three different scavengers, namely tetramethylpiperidine-N-oxyl (TEMPO), thiophenol (PhSH), and β-mercaptoethanol (BME), and detailed analysis of products was performed. NMR differentiates between N-inversion, epimerization, and homolysis reactions. The choice of scavenger is crucial for making a reliable and accurate estimate of the true homolysis rate constant.


2004 ◽  
Vol 287 (4) ◽  
pp. E652-E661 ◽  
Author(s):  
Daniel M. Keenan ◽  
Ferdinand Roelfsema ◽  
Johannes D. Veldhuis

According to current regulatory concepts, pulsatile ACTH concentrations (CON) stimulate time-lagged cortisol secretion rates (SEC) via an implicit CON-SEC dose-response relationship. The present analyses reconstruct nonlinear properties of this in vivo agonist-response interface noninvasively in order to investigate pulse-by-pulse coupling consistency and to obviate the need to infuse isotopes or exogenous effectors, which may disrupt pathway interactions. This approach required an ensemble strategy of 1) measuring ACTH and cortisol CON in plasma sampled every 10 min for 24 h in 32 healthy adults, and 2) estimating simultaneously a) variable-waveform ACTH and cortisol SEC bursts superimposed upon fixed basal SEC; b) biexponential kinetics of ACTH and cortisol disappearance; c) nonequilibrium exchange of cortisol among free and cortisol-binding globulin (CBG)- and albumin-bound moieties; d) two SEC-burst shapes demarcated by a statistically defined day/night boundary; e) feedforward efficacy, potency, and sensitivity; and f) stochastic variability in feedforward measures over time. Thereby, we estimate 1) ACTH SEC (μg·l−1·day−1) of 0.27 ± 0.04 basal and 0.87 ± 0.07 pulsatile (means ± SE); 2) cortisol SEC (μmol·l−1·day−1) of 0.10 ± 0.01 basal and 3.5 ± 0.20 pulsatile; 3) free cortisol half-lives (min) of 1.8 ± 0.20 (diffusion/advection) and 4.1 ± 0.30 (elimination) and a half-life of total cortisol of 49 ± 2.4 and of ACTH of 20 ± 1.3; 4) ACTH potency (EC50, ng/l) of 26 ± 2.4, efficacy (nmol·l−1·min−1) 10 ± 1.8, and sensitivity (slope units) 0.65 ± 0.09; 5) night/day augmentation of ACTH and cortisol SEC-burst mass by 2.1- and 1.7-fold (median); 6) abbreviation of the modal time to maximal ACTH and cortisol SEC rates by 4.4- and 4.3-fold, respectively, after a change point clock time of 0205 (median); 7) in vivo percentage distribution of cortisol as 6% free, 14% albumin bound, and 80% CBG bound with an absolute free cortisol CON (nmol/l) 11.5 ± 0.54; and 8) significant (mean CV) stochastic variability in feedforward efficacy (140%), potency (38%), and sensitivity (56%) within the succession of paired ACTH/cortisol pulses of any given subject. In conclusion, the present composite formulation illustrates a platform for dissecting mechanisms of in vivo regulation of effector-response properties noninvasively in the corticotropic axis of the uninfused individual.


2002 ◽  
Vol 361 (2) ◽  
pp. 355-361 ◽  
Author(s):  
Luis M. BREDESTON ◽  
Alcides F. REGA

Pre-steady-state phosphorylation and dephosphorylation of purified and phospholipid-depleted plasma-membrane Ca2+-ATPase (PMCA) solubilized in the detergent polyoxyethylene 10 lauryl ether were studied at 25°C. The time course of phosphorylation with ATP of the enzyme associated with Ca2+, probably the true phosphorylation reaction, showed a fast phase (kapp near 400s−1) followed by a slow phase (kapp = 23s−1). With asolectin or acidic phosphatidylinositol, the concentration of phosphoenzyme (EP) increased at as high a rate as before, passed through a maximum at 4ms and stabilized at a steady level that was approx. half that without lipids. Calmodulin (CaM) did not change the rate of the fast phase, accelerated the slow phase (kapp = 93s−1) and increased [EP] with small changes in the shape of the time course. Dephosphorylation was slow (kapp = 30s−1) and insensitive to CaM. Asolectin accelerated dephosphorylation, which followed biexponential kinetics with fast (kapp = 220s−1) and slow (kapp = 20s−1) components. CaM stimulated the fast component by nearly 50%. The results show that the behaviour of the PMCA is complex, and suggest that acidic phospholipids and CaM activate PMCA through different mechanisms. Acceleration of dephosphorylation seems relevant during activation of the PMCA by acidic phospholipids.


1990 ◽  
Vol 55 (5) ◽  
pp. 1612-1616 ◽  
Author(s):  
Robert E. West ◽  
Adam Zweig ◽  
Russell T. Granzow ◽  
Marvin I. Siegel ◽  
Robert W. Egan

Sign in / Sign up

Export Citation Format

Share Document