A temperature-jump stopped-flow system for monitoring chemical kinetics triggered by rapid cooling

Talanta ◽  
2007 ◽  
Vol 71 (3) ◽  
pp. 1276-1281 ◽  
Author(s):  
Brian L. Boys ◽  
Lars Konermann
Keyword(s):  
Chemical Kinetics ◽  
Temperature Jump ◽  
Flow System ◽  
Stopped Flow ◽  
Rapid Cooling

scholarly journals Time-resolved detection of SDS-induced conformational changes in α-synuclein by a micro-stopped-flow system

RSC Advances ◽  
2021 ◽  
Vol 11 (2) ◽  
pp. 1086-1097
Author(s):  
Shunki Takaramoto ◽  
Yusuke Nakasone ◽  
Kei Sadakane ◽  
Shinsaku Maruta ◽  
Masahide Terazima
Keyword(s):  
Conformational Changes ◽  
Flow System ◽  
Stopped Flow ◽  
Time Resolved ◽  
Sds Micelles ◽  
Conformation Changes ◽  
System P

Dynamics of conformation changes of α-synuclein induced by the presence of SDS micelles are revealed using time-resolved diffusion, CD, and FRET measurements combined with a micro-stopped flow system.

scholarly journals A micro-volume adaptation of a stopped-flow system; use with μg quantities of muscle proteins

2019 ◽  
Vol 581 ◽  
pp. 113338
Author(s):  
J. Walklate ◽  
Zoltan Ujfalusi ◽  
Vincent Behrens ◽  
Edward J. King ◽  
Michael A. Geeves
Keyword(s):  
Flow System ◽  
Stopped Flow ◽  
Muscle Proteins ◽  
System Use

Stopped-flow measurements of CO and O2 uptake by hemoglobin in sheep erythrocytes

1963 ◽  
Vol 18 (1) ◽  
pp. 158-165 ◽  
Author(s):  
John A. Sirs ◽  
F. J. W. Roughton
Keyword(s):  
Linear Relation ◽  
Flow System ◽  
Stopped Flow ◽  
Constant Flow ◽  
Dissolved Gas ◽  
O2 Uptake ◽  
Flow Measurements ◽  
Sheep Erythrocytes ◽  
Flow Method ◽  
Comparison Of The Results

A stopped-flow method is described to measure spectrophotometrically the rates of uptake of CO and O2 by the hemoglobin of intact sheep erythrocytes. A comparison of the results obtained with the constant flow system has led to further refinement of the latter procedure. A linear relation is found between the rate of uptake and the concentration of the dissolved gas, and the initial percentage rate of saturation is independent of the concentration of the erythrocytes. Submitted on September 21, 1961

scholarly journals Enzyme Kinetics above Denaturation Temperature: A Temperature-Jump/Stopped-Flow Apparatus

2006 ◽  
Vol 91 (12) ◽  
pp. 4605-4610 ◽  
Author(s):  
Bálint Kintses ◽  
Zoltán Simon ◽  
Máté Gyimesi ◽  
Júlia Tóth ◽  
Balázs Jelinek ◽  
...  
Keyword(s):  
Enzyme Kinetics ◽  
Temperature Jump ◽  
Stopped Flow ◽  
Denaturation Temperature ◽  
Flow Apparatus

Etude cinétique des systèmes Cu(II)•Adénosine et Cu(II)•D-Ribose

1972 ◽  
Vol 50 (19) ◽  
pp. 3117-3123 ◽  
Author(s):  
G. Boivin ◽  
M. Zador
Keyword(s):  
Kinetic Parameters ◽  
Acidic Medium ◽  
Temperature Jump ◽  
Strong Acid ◽  
Basic Medium ◽  
Stopped Flow ◽  
Acid Solutions ◽  
Flow Method ◽  
Kinetics Of ◽  
Adenine Base

The kinetics of the formation and dissociation of Cu(II) complexes of adenosine have been determined in acidic and basic medium. In acidic medium, the complex is formed between the Cu(II) and the adenine base and the kinetic parameters have been obtained in this case using a temperature jump method. In basic medium, only the dissociation of the complexes could be studied by a stopped-flow method, by addition of EDTA or strong acid solutions. In these complexes, Cu(II) is bridged with ribose hydroxyls. Finally, D-ribose has also been studied for comparison in the same conditions. The mechanism of these reactions is discussed.

scholarly journals Studies on partially reduced mammalian cytochrome oxidase reactions with ferrocytochrome c

1976 ◽  
Vol 157 (3) ◽  
pp. 591-598 ◽  
Author(s):  
C Greenwood ◽  
T Brittain
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Cytochrome Oxidase ◽  
Transfer Reaction ◽  
Temperature Jump ◽  
Electron Transfer Reaction ◽  
Relaxation Processes ◽  
Stopped Flow ◽  
Rapid Reduction ◽  
Ferrocytochrome C

The kinetics of the electron-transfer process which occurs between ferrocytochrome c and partially reduced mammalian cytochrome oxidase were studied by the rapid spectrophotometric techniques of stopped flow and temperature jump. Stopped-flow experiments showed initial very fast extinction changes at 605 nm and at 563 nm, indicating the simultaneous reduction of cytochrome a and oxidation of ferrocytochrome c. During this ‘burst’ phase, say the first 50 ms after mixing, it was invariably found that more cytochrome c had been oxidized than cytochrome a had been reduced. This discrepancy in electron equivalents may be accounted for by the rapid reduction of another redox site in the enzyme, possibly that associated with the extinction changes observed at 830 nm. During the incubation period in which the partially reduced oxidase was prepared, the rate of reduction of cytochrome a by ferrocytochrome c, at constant reactant concentrations, decreased with time. Temperature-jump experiments showed the presence of two relaxation processes. The faster of the two phases was assigned to the electron-transfer reaction between cytochrome c and cytochrome a. A study of the concentration-dependence of the reciprocal relaxation time for this phase yielded a rate constant of 9 X 10(6)M-1-s-1 for the electron transfer from cytochrome c to cytochrome a, and a value of 8.5 X 10(6)M-1-s-1 for the reverse reaction. The equilibrium constant for the electron-transfer reaction is therefore close to unity. The slower phase has been interpreted as signalling the transfer of electrons between cytochrome a and another redox site within the oxidase molecule.

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