Membrane Fractionation of Liquors from Lignin‐First Biorefining

ChemSusChem ◽  
2019 ◽  
Vol 12 (6) ◽  
pp. 1203-1212 ◽  
Author(s):  
Zafar Sultan ◽  
Inês Graça ◽  
Yueqin Li ◽  
Sérgio Lima ◽  
Ludmila G. Peeva ◽  
...  

2018 ◽  
Vol 197 ◽  
pp. 360-371 ◽  
Author(s):  
Inês Ferreira Mota ◽  
Paula Rodrigues Pinto ◽  
Ana Mafalda Ribeiro ◽  
José Miguel Loureiro ◽  
Alírio Egídio Rodrigues


2008 ◽  
Vol 131 (6) ◽  
pp. 617-627 ◽  
Author(s):  
Gustavo Frindt ◽  
Zuhal Ergonul ◽  
Lawrence G. Palmer

Expression of epithelial Na channel (ENaC) protein in the apical membrane of rat kidney tubules was assessed by biotinylation of the extracellular surfaces of renal cells and by membrane fractionation. Rat kidneys were perfused in situ with solutions containing NHS-biotin, a cell-impermeant biotin derivative that attaches covalently to free amino groups on lysines. Membranes were solubilized and labeled proteins were isolated using neutravidin beads, and surface β and γENaC subunits were assayed by immunoblot. Surface αENaC was assessed by membrane fractionation. Most of the γENaC at the surface was smaller in molecular mass than the full-length subunit, consistent with cleavage of this subunit in the extracellular moiety close to the first transmembrane domains. Insensitivity of the channels to trypsin, measured in principal cells of the cortical collecting duct by whole-cell patch-clamp recording, corroborated this finding. ENaC subunits could be detected at the surface under all physiological conditions. However increasing the levels of aldosterone in the animals by feeding a low-Na diet or infusing them directly with hormone via osmotic minipumps for 1 wk before surface labeling increased the expression of the subunits at the surface by two- to fivefold. Salt repletion of Na-deprived animals for 5 h decreased surface expression. Changes in the surface density of ENaC subunits contribute significantly to the regulation of Na transport in renal cells by mineralocorticoid hormone, but do not fully account for increased channel activity.



2016 ◽  
Vol 94 (suppl_5) ◽  
pp. 248-248 ◽  
Author(s):  
L. D. Alexander ◽  
M. A. Stout ◽  
M. Drake ◽  
S. L. Beckman ◽  
L. Metzger


1973 ◽  
Vol 300 (3) ◽  
pp. 211-254 ◽  
Author(s):  
D.F. Hoelzl Wallach ◽  
Peck Sun Lin


2021 ◽  
Vol 9 (2) ◽  
pp. 418
Author(s):  
Mikhail Oliveira Leastro ◽  
Juliana Freitas-Astúa ◽  
Elliot Watanabe Kitajima ◽  
Vicente Pallás ◽  
Jesús Á. Sánchez-Navarro

Although citrus leprosis disease has been known for more than a hundred years, one of its causal agents, citrus leprosis virus C2 (CiLV-C2), is poorly characterized. This study described the association of CiLV-C2 movement protein (MP) and capsid protein (p29) with biological membranes. Our findings obtained by computer predictions, chemical treatments after membrane fractionation, and biomolecular fluorescence complementation assays revealed that p29 is peripherally associated, while the MP is integrally bound to the cell membranes. Topological analyses revealed that both the p29 and MP expose their N- and C-termini to the cell cytoplasmic compartment. The implications of these results in the intracellular movement of the virus were discussed.



2006 ◽  
Vol 9 (1) ◽  
Author(s):  
Fengqin Wang ◽  
Daniel W. Smith ◽  
Mohamed Gamal El-Din

AbstractTreatment of an aged raw landfill leachate with H



Planta ◽  
1998 ◽  
Vol 205 (3) ◽  
pp. 380-388 ◽  
Author(s):  
Adrian Turner ◽  
Antony Bacic ◽  
Philip J. Harris ◽  
Steve M. Read




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