Redox catalysis has been broadly utilized in electrochemical synthesis due to its kinetic advantages over direct electrolysis. The appropriate choice can avoid electrode passivation, which strongly inhibit the efficient activation of substrates. 14215-68-0, Name is N-((2S,3R,4R,5R,6R)-2,4,5-Trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-3-yl)acetamide, molecular formula is C8H15NO6. In a Article，once mentioned of 14215-68-0, Electric Literature of 14215-68-0
The cells of the human monocytic leukemia cell line THP-1 differentiated into macrophages bound to human erythrocytes oxidized with adenosine 5′- diphosphate (ADP)-Fe3+ chelate (ADP/Fe3+) in the absence of serum. The binding was prevented when the cells were treated with ADP/Fe3+ in the presence of antioxidants, indicating that oxidation of the cells is responsible for the increased susceptibility to the THP-1 cell binding. Galactose, fucose, mannose and mannan partially inhibited the binding. Glycoproteins containing poly-N-acetyllactosaminyl saccharide chains such as band 3 glycoprotein isolated from human erythrocyte membrane and lactoferrin, and their oligosaccharides, strongly inhibited the binding. On the other hand, glycoproteins with non-poly-N-acetyllactosaminyl saccharide chains such as glycophorin A isolated from the erythrocyte membrane, fetuin and alpha1- acid glycoprotein, little or partially inhibited the binding. The inhibitory activity of band 3 oligosaccharides and lactoferrin oligosaccharides was little affected by treatment with endo-beta-galactosidase, which specifically cleaves poly-N-acetyllactosamine to shorter oligosaccharides. Removal of the nonreducing terminal region of the saccharide chains of band 3 on the erythrocyte surface by treatment of the cells with endo-beta-galactosidase resulted in a decrease in the susceptibility of the cells to the THP-1 cell binding. These results suggest that THP-1 cells which have been differentiated into macrophages bind the oxidized erythrocytes primarily through the recognition of poly-N-acetyllactosaminyl saccharide chains of band 3, and the site of the recognition exists in the nonreducing terminal region of the saccharide chains. Clustering of band 3 molecules is proposed as a possible alteration of oxidized erythrocyte membrane which promotes the interaction of the saccharide receptor on THP-1 cells with the saccharide chains of band 3 on erythrocytes.
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Reference：
Tetrahydropyran – Wikipedia,
Tetrahydropyran – an overview | ScienceDirect Topics