Oxygen Sensing in Nonaqueous Media Using Porous Glass with Covalently Bound Luminescent Ru(II) Complexes

1998 ◽  
Vol 70 (24) ◽  
pp. 5184-5189 ◽  
Author(s):  
María P. Xavier ◽  
David García-Fresnadillo ◽  
María C. Moreno-Bondi ◽  
Guillermo Orellana
2014 ◽  
Vol 2 (36) ◽  
pp. 7589-7598 ◽  
Author(s):  
L. H. Hutter ◽  
B. J. Müller ◽  
K. Koren ◽  
S. M. Borisov ◽  
I. Klimant

New high performance optical oxygen sensing materials based on NIR-emitting indicators covalently bound to various polymers overcome main limitations of the conventional sensors.


2010 ◽  
Vol 48 (3) ◽  
pp. 663-670 ◽  
Author(s):  
Makoto Obata ◽  
Noriko Matsuura ◽  
Kazunori Mitsuo ◽  
Hiroki Nagai ◽  
Keisuke Asai ◽  
...  

2000 ◽  
Vol 14 (12) ◽  
pp. 895-905 ◽  
Author(s):  
Marı́a P Xavier ◽  
Begoña Vallejo ◽  
Marı́a D Marazuela ◽  
Marı́a C Moreno-Bondi ◽  
F Baldini ◽  
...  

1973 ◽  
Vol 38 (7) ◽  
pp. 2011-2015 ◽  
Author(s):  
T. Barth ◽  
K. Jošt ◽  
I. Rychlík

1972 ◽  
Vol 14 (3) ◽  
pp. 509-513 ◽  
Author(s):  
G. W. Strandberg ◽  
K. L. Smiley

1979 ◽  
Vol 41 (04) ◽  
pp. 687-690
Author(s):  
F R Matthias

SummaryAfter thrombin treatment insolubilized fibrinmonomer, which is obtained from insolubilized fibrinogen covalently bound to agarose, adsorbs soluble fibrin and its derivatives from solutions. The immobilized proteins are attached to the agarose by the ‘A’ αchain. After reduction of the disulfide bridges the β and γchains can be removed from the agarose.After thrombin treatment the immobilized αchain adsorbs fibrinogen and fragment D. To some extent the β and γchain do not seem necessary for the adsorption. The amount adsorbed increases, when thrombin treatment of the insolubilized protein follows the reduction process.This may indicate that the fibrinopeptides ‘A’ of the insolubilized αchain are better accessible after the removal of the β and γchains.


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