An infrared assay of the kinetics of phosphate-release from physiological substrates in living cells

2014 ◽  
Author(s):  
Ren Zhongyuan ◽  
Do Leduy ◽  
Saida Mebarek ◽  
Nermin Keloglu ◽  
Saandia Ahamada ◽  
...  
Keyword(s):  
Living Cells ◽  
Phosphate Release ◽  
Kinetics Of ◽  
Physiological Substrates

Spectrochemical Behavior of Carcinogenic Polycyclic Aromatic Hydrocarbons in Biological Systems. Part II: A Theoretical Rate Model for BaP Metabolism in Living Cells

1996 ◽  
Vol 50 (11) ◽  
pp. 1352-1359 ◽  
Author(s):  
Ping Chiang ◽  
Kuang-Pang Li ◽  
Tong-Ming Hseu
Keyword(s):  
Rate Constant ◽  
Living Cells ◽  
Rate Model ◽  
Number Density ◽  
Order Process ◽  
Irreversible Reaction ◽  
First Order ◽  
Metabolism Rate ◽  
Polycyclic Aromatic ◽  
Kinetics Of

An idealized model for the kinetics of benzo[ a]pyrene (BaP) metabolism is established. As observed from experimental results, the BaP transfer from microcrystals to the cell membrane is definitely a first-order process. The rate constant of this process is signified as k1. We describe the surface–midplane exchange as reversible and use rate constants k2 and k3 to describe the inward and outward diffusions, respectively. The metabolism is identified as an irreversible reaction with a rate constant k4. If k2 and k3 are assumed to be fast and not rate determining, the effect of the metabolism rate, k4, on the number density of BaP in the midplane of the microsomal membrane, m3, can be estimated. If the metabolism rate is faster than or comparable to the distribution rates, k2 and k3, the BaP concentration in the membrane midplane, m3, will quickly be dissipated. But if k4 is extremely small, m3 will reach a plateau. Under conditions when k2 and k3 also play significant roles in determining the overall rate, more complicated patterns of m3 are expected.

scholarly journals THE KINETICS OF EXOSMOSIS OF WATER FROM LIVING CELLS

1927 ◽  
Vol 10 (5) ◽  
pp. 659-664 ◽  
Author(s):  
Morton McCutcheon ◽  
Baldwin Lucke
Keyword(s):  
Osmotic Pressure ◽  
Salt Concentration ◽  
Driving Force ◽  
Temperature Characteristic ◽  
Living Cells ◽  
Velocity Constant ◽  
Osmotic Equilibrium ◽  
Kinetics Of

1. The rate of exosmosis of water was studied in unfertilized Arbacia eggs, in order to bring out possible differences between the kinetics of exosmosis and endosmosis. 2. Exosmosis, like endosmosis, is found to follow the equation See PDF for Equation, in which a is the total volume of water that will leave the cell before osmotic equilibrium is attained, x is the volume that has already left the cell at time t, and k is the velocity constant. 3. The velocity constants of the two processes are equal, provided the salt concentration of the medium is the same. 4. The temperature characteristic of exosmosis, as of endomosis, is high. 5. It is concluded that the kinetics of exosmosis and endosmosis of water in these cells are identical, the only difference in the processes being in the direction of the driving force of osmotic pressure.

scholarly journals Localization and Kinetics of Reduced Pyridine Nucleotide in Living Cells by Microfluorometry

1959 ◽  
Vol 234 (11) ◽  
pp. 3044-3050
Author(s):  
Britton Chance ◽  
Bo Thorell
Keyword(s):  
Pyridine Nucleotide ◽  
Living Cells ◽  
Kinetics Of

scholarly journals Effects of Ca2+ on the kinetics of phosphate release in skeletal muscle.

1992 ◽  
Vol 267 (4) ◽  
pp. 2459-2466 ◽  
Author(s):  
J W Walker ◽  
Z Lu ◽  
R L Moss
Keyword(s):  
Skeletal Muscle ◽  
Phosphate Release ◽  
Kinetics Of

scholarly journals SIMILARITY OF THE KINETICS OF INVERTASE ACTION IN VIVO AND IN VITRO. II

1932 ◽  
Vol 16 (2) ◽  
pp. 233-242 ◽  
Author(s):  
B. G. Wilkes ◽  
Elizabeth T. Palmer
Keyword(s):  
Physiological Activity ◽  
Outer Region ◽  
Living Cells ◽  
Yeast Cells ◽  
Live Cells ◽  
Intracellular Enzyme ◽  
Relationship Of ◽  
Kinetics Of

1. The pH-activity relationship of invertase has been studied in vivo and in vitro under identical external environmental conditions. 2. The effect of changing (H+) upon the sucroclastic activity of living cells of S. cerevisiae and of invertase solutions obtained therefrom has been found, within experimental error, to be identical. 3. The region of living yeast cells in which invertase exerts its physiological activity changes its pH freely and to the same extent as that of the suspending medium. It is suggested that this may indicate that this intracellular enzyme may perform its work somewhere in the outer region of the cell. 4. In using live cells containing maltase, no evidence of increased sucroclastic activity around pH 6.9, due to the action of Weidenhagen's α-glucosidase (maltase), was found.

scholarly journals Development of mKO2 fusion proteins for real-time imaging and mechanistic investigation of the degradation kinetics of human IκBα in living cells

2019 ◽  
Vol 1866 (2) ◽  
pp. 190-198
Author(s):  
Nilufar Rahimova ◽  
Hasan Babazada ◽  
Yuriko Higuchi ◽  
Fumiyoshi Yamashita ◽  
Mitsuru Hashida
Keyword(s):  
Real Time ◽  
Fusion Proteins ◽  
Degradation Kinetics ◽  
Living Cells ◽  
Real Time Imaging ◽  
Mechanistic Investigation ◽  
Kinetics Of

Quantifying Target Occupancy of Small Molecules Within Living Cells

2020 ◽  
Vol 89 (1) ◽  
pp. 557-581 ◽  
Author(s):  
M.B. Robers ◽  
R. Friedman-Ohana ◽  
K.V.M. Huber ◽  
L. Kilpatrick ◽  
J.D. Vasta ◽  
...  
Keyword(s):  
Cultured Cells ◽  
Drug Efficacy ◽  
Living Cells ◽  
Drug Binding ◽  
Therapeutic Window ◽  
Target Engagement ◽  
Binding Properties ◽  
Structure Activity ◽  
Sar Analysis ◽  
Kinetics Of

The binding affinity and kinetics of target engagement are fundamental to establishing structure–activity relationships (SARs) for prospective therapeutic agents. Enhancing these binding parameters for operative targets, while minimizing binding to off-target sites, can translate to improved drug efficacy and a widened therapeutic window. Compound activity is typically assessed through modulation of an observed phenotype in cultured cells. Quantifying the corresponding binding properties under common cellular conditions can provide more meaningful interpretation of the cellular SAR analysis. Consequently, methods for assessing drug binding in living cells have advanced and are now integral to medicinal chemistry workflows. In this review, we survey key technological advancements that support quantitative assessments of target occupancy in cultured cells, emphasizing generalizable methodologies able to deliver analytical precision that heretofore required reductionist biochemical approaches.

scholarly journals Activation Kinetics of RAF Protein in the Ternary Complex of RAF, RAS-GTP, and Kinase on the Plasma Membrane of Living Cells

2011 ◽  
Vol 286 (42) ◽  
pp. 36460-36468 ◽  
Author(s):  
Kayo Hibino ◽  
Tatsuo Shibata ◽  
Toshio Yanagida ◽  
Yasushi Sako
Keyword(s):  
Plasma Membrane ◽  
Ternary Complex ◽  
Living Cells ◽  
Activation Kinetics ◽  
Kinetics Of

Kinetics of M1muscarinic receptor and G protein signaling to phospholipase C in living cells

2010 ◽  
Vol 188 (3) ◽  
pp. i5-i5
Author(s):  
Björn H. Falkenburger ◽  
Jill B. Jensen ◽  
Bertil Hille
Keyword(s):  
Phospholipase C ◽  
G Protein ◽  
Living Cells ◽  
G Protein Signaling ◽  
Protein Signaling ◽  
Kinetics Of
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