A heterobifunctional cross-linking reagent containing a sulfhydryl-specific group and a photo-active group. Typically, coupled initially by thioether to molecule containing free sulfhydryl buffered at pH 6.8 (6.5-7.0). Second bonding occurs during UV irradiation (250 nm) via diradical excited state. Benzophenones demonstrate greater specificity for C-H insertion and are more stable in water than analogous reagents. In general they are more efficient in attachment because they may be repeatedly irradiated; however, a more intense irradiation may be required. The benzophenone is not sensitive to reduction compared to analogous reagents.
It has been shown that the EGTA-resistant actin, one of the two actin molecules associated to gelsolin, can be predominantly cross-linked to gelsolin by benzophenone-4-maleimide (BPM), a photoaffinity-labeling reagent, which was conjugated to Cys-374 of actin prior to cross-linking (Doi
To attain light-dependent functionalization of biocompatible materials, a photolabel-derivatized, bioactive laminin fragment has been synthesized, chemically characterized, and photoimmobilized. Covalent high-resolution patterning of the laminin fragment CDPGYIGSR to hydroxylated fluorinated ethylene propylene (FEP-OH), poly(vinyl alcohol), and glycophase glass has been
The Journal of biological chemistry, 280(30), 27896-27903 (2005-06-14)
The vacuolar (H+)-ATPases (V-ATPases) are multisubunit complexes responsible for ATP-dependent proton transport across both intracellular and plasma membranes. The V-ATPases are composed of a peripheral domain (V1) that hydrolyzes ATP and an integral domain (V0) that conducts protons. Dissociation of
LEC-1 is the first tandem repeat-type galectin isolated from an animal system; this galectin has two carbohydrate recognition domains in a single polypeptide chain. Because its two lectin domains have different sugar-binding profiles, these domains are thought to interact with
The Journal of biological chemistry, 272(47), 29518-29526 (1997-12-31)
Bacterial detoxification of mercuric ion depends on the presence of one or more integral membrane proteins (MerT and/or MerC) whose postulated function is in transport of Hg2+ from a periplasmic Hg2+-binding protein (MerP) to cytoplasmic mercuric reductase. In this study
Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..
