Does the Reconstitution of RC-LH1 Complexes from Rhodopseudomonas acidophila Strain 10050 into a Phospholipid Bilayer Yield the Optimum Environment for Optical Spectroscopy?

2013 ◽  
Vol 117 (48) ◽  
pp. 15004-15013 ◽  
Author(s):  
Paul S. Böhm ◽  
Ralf Kunz ◽  
June Southall ◽  
Richard J. Cogdell ◽  
Jürgen Köhler

1991 ◽  
Vol 65 (02) ◽  
pp. 139-143 ◽  
Author(s):  
Cynthia H Gemmell ◽  
Vincet T Turitto ◽  
Yale Nemerson

SummaryA novel reactor recently described for studying phospholipiddependent blood coagulation reactions under flow conditions similar to those occurring in the vasculature has been further charactenzed. The reactor is a capitlary whose inner wall is coated with a stable phospholipid bilayer (or two bilayers) containing tissue factor, a transmembrane protein that is required for the enzymatic activation of factor X by factor VIIa. Perfusion of the capillary at wall shear rates ranging from 25 s−1 to 1,200 s−1 with purified bovine factors X and VIIa led to steady state factor Xa levels at the outlet. Assay were performed using a chromogenic substrate, SpectrozymeTMFXa, or by using a radiometric technique. In the absence of Ca2+ or factor VIIa there was no product formation. No difference was noted in the levels of factor Xa achieved when non-activated factor VII was perfused. Once steady state was achieved further factor Xa production continued in the absence of factor VIIa implying a very strong association of factor VIIa with the tissue factor in the phospholipid membrane. In agreement with static vesicle-type studies the reactor was sensitive to wall tissue factor concentration, temperature and the presence of phosphatidylserine in the bilayer.



2006 ◽  
Vol 49 (1) ◽  
pp. 25-35 ◽  
Author(s):  
Mauro Missori ◽  
Marcofabio Righini


2016 ◽  
Vol 19 (4) ◽  
pp. 319-324 ◽  
Author(s):  
Blanka Ziomkowska ◽  
Tomasz Wybranowski ◽  
Michal Cyrankiewicz ◽  
Stefan Kruszewski
Keyword(s):  


Author(s):  
Aline E. Casaril ◽  
Carlos G. Santos ◽  
Bruno S. Marangoni ◽  
Sandro M. Lima ◽  
Luis H.C. Andrade ◽  
...  


2017 ◽  
Vol 1 (4) ◽  
Author(s):  
Lei Zhang ◽  
X. Fu ◽  
M. Hohage ◽  
P. Zeppenfeld ◽  
L. D. Sun


Author(s):  
Austin M. Wallace ◽  
Christine Curiac ◽  
Jared H. Delcamp ◽  
Ryan C. Fortenberry


2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Koshi Nishida ◽  
Toshifumi Tojo ◽  
Takeshi Kondo ◽  
Makoto Yuasa

AbstractPorphyrin derivatives accumulate selectively in cancer cells and are can be used as carriers of drugs. Until now, the substituents that bind to porphyrins (mainly at the meso-position) have been actively investigated, but the effect of the functional porphyrin positions (β-, meso-position) on tumor accumulation has not been investigated. Therefore, we investigated the correlation between the functional position of substituents and the accumulation of porphyrins in cancer cells using cancer cells. We found that the meso-derivative showed higher accumulation in cancer cells than the β-derivative, and porphyrins with less bulky substituent actively accumulate in cancer cells. When evaluating the intracellular distribution of porphyrin, we found that porphyrin was internalized by endocytosis and direct membrane permeation. As factors involved in these two permeation mechanisms, we evaluated the affinity between porphyrin-protein (endocytosis) and the permeability to the phospholipid bilayer membrane (direct membrane permeation). We found that the binding position of porphyrin affects the factors involved in the transmembrane permeation mechanisms and impacts the accumulation in cancer cells.



Author(s):  
C. Robert ◽  
M. A. Semina ◽  
F. Cadiz ◽  
M. Manca ◽  
E. Courtade ◽  
...  


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