Validation of a Hyperspectral NIRS Method for Measuring Oxygen Saturation by Comparison to Time-Resolved NIRS

Author(s):  
Matthew D. Kewin ◽  
Daniel F. Milej ◽  
Androu Abdalmalak ◽  
Ajay Rajaram ◽  
Mamadou Diop ◽  
...  
2013 ◽  
Vol 25 (3) ◽  
pp. 248-253 ◽  
Author(s):  
Kenji Yoshitani ◽  
Ken Kuwajima ◽  
Tomoya Irie ◽  
Yuzuru Inatomi ◽  
Atushi Miyazaki ◽  
...  

1993 ◽  
Vol 47 (10) ◽  
pp. 1604-1608 ◽  
Author(s):  
Ruixia Song ◽  
Kuang-Pang Li

Benzo(a)pyrene (BP) in liposomes and microsomes exhibits overlapping excimer bands peaked at 495 and 520 nm, respectively, in contrast to the single band of pyrene at 480 nm. Since BP is asymmetrical and pyrene is symmetrical, the dual maxima imply that the BP molecules in the excimer must be oriented either parallel or anti-parallel to each other. Time-resolved studies of BP oxidation by cytochrome P-450 show that the 520-nm component dissipates much faster than the 495-nm component during the first 30 min of metabolism, indicating that the initial P-450-BP interaction may be BP orientation sensitive. The binding of BP to the porphyrin group of a heme protein (e.g., hemoglobin or myoglobin) appears to be stronger under oxygen saturation than under CO2 saturation conditions. The transfer of BP between the membrane and the porphyrin group, as measured by means of excimer/monomer ratios, appears to be significantly different from that of pyrene. As the liposome-to-protein ratio increases, the excimer/monomer of BP steadily decreases, whereas that of pyrene increases and reaches a plateau. The significance of this phenomenon in their mechanisms of metabolism will have to be investigated further.


2019 ◽  
Vol 10 (9) ◽  
pp. 4789 ◽  
Author(s):  
Matthew Kewin ◽  
Ajay Rajaram ◽  
Daniel Milej ◽  
Androu Abdalmalak ◽  
Laura Morrison ◽  
...  

Author(s):  
Elizabeth M. C. Hillman ◽  
Simon. R. Arridge ◽  
Jeremy C. Hebden ◽  
David T. Delpy

2015 ◽  
Vol 37 (10) ◽  
pp. 925-932 ◽  
Author(s):  
Shinji Nakamura ◽  
Kosuke Koyano ◽  
Wataru Jinnai ◽  
Satoshi Hamano ◽  
Saneyuki Yasuda ◽  
...  

Author(s):  
Eva-Maria Mandelkow ◽  
Eckhard Mandelkow ◽  
Joan Bordas

When a solution of microtubule protein is changed from non-polymerising to polymerising conditions (e.g. by temperature jump or mixing with GTP) there is a series of structural transitions preceding microtubule growth. These have been detected by time-resolved X-ray scattering using synchrotron radiation, and they may be classified into pre-nucleation and nucleation events. X-ray patterns are good indicators for the average behavior of the particles in solution, but they are difficult to interpret unless additional information on their structure is available. We therefore studied the assembly process by electron microscopy under conditions approaching those of the X-ray experiment. There are two difficulties in the EM approach: One is that the particles important for assembly are usually small and not very regular and therefore tend to be overlooked. Secondly EM specimens require low concentrations which favor disassembly of the particles one wants to observe since there is a dynamic equilibrium between polymers and subunits.


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