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.
The interaction of the membrane traversing stator subunits a and b of the rotary ATP synthase was probed by substitution of a single Cys into each subunit with subsequent Cu(2+) catalyzed cross-linking. Extensive interaction between the transmembrane (TM) region of
Biochemical and biophysical research communications, 390(3), 581-584 (2009-10-13)
Relatively weak interactions between galectins and their potential ligands can hinder identification of physiological lectin ligands using conventional methods such as affinity purification. We have employed a combination of cysteine mutagenesis with chemical crosslinking using a photoactivatable sulfhydryl reagent benzophenone-4-maleimide
To investigate protein-protein interaction sites in the DNA mismatch repair system we developed a crosslinking/mass spectrometry technique employing a commercially available trifunctional crosslinker with a thiol-specific methanethiosulfonate group, a photoactivatable benzophenone moiety and a biotin affinity tag. The XACM approach
Radionuclide molecular imaging of cancer-specific targets is a promising method to identify patients for targeted antibody therapy. Radiolabeled full-length antibodies however suffer from slow clearance, resulting in high background radiation. To overcome this problem, a pretargeting system based on complementary
Archives of biochemistry and biophysics, 288(2), 584-590 (1991-08-01)
Experimental conditions which permit the exchange of smooth muscle 20-kDa light chain into skeletal muscle myosin are described. The hybridization does not result in the regulation of actin-activated ATPase activity of the hybrid myosin by smooth light chain phosphorylation. Further
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