The Journal of biological chemistry, 262(13), 6128-6134 (1987-05-05)
Electron microscopy studies have shown that the structure of the complex of myosin subfragment 1 (S-1) cross-linked to actin with 1-ethyl-3-[3-(dimethyl-amino) propyl] carbodiimide is very different in the presence and absence of ATP (Craig, R., Greene, L. E., and Eisenberg
In our previous study [Chalovich, J. M., Greene, L. E., & Eisenberg, E. (1983) Proc. Natl. Acad. Sci. U.S.A. 80, 4909-4913], myosin subfragment 1 that was modified by having its two reactive thiol groups cross-linked by N,N'-p-phenylenedimaleimide (pPDM) was found
European journal of biochemistry, 227(1-2), 459-465 (1995-01-15)
Porcine aorta myosin was reacted with a bifunctional cross-linking reagent, N,N'-o-phenylenedimaleimide. The 17-kDa essential light chain (LC17) in each myosin head was intramolecularly cross-linked within a single myosin molecule. The 34-kDa cross-linked LC17 dimer was isolated and its peptide map
Proceedings of the National Academy of Sciences of the United States of America, 81(21), 6599-6602 (1984-11-01)
The bifunctional reagent N,N'-p-phenylenedimaleimide (PDM) is being used in an attempt to measure distances between specific side chains in adjacent monomers within F-actin. [14C]PDM was synthesized and was used to crosslink F-actin. Uncrosslinked actin was removed by gel filtration, and
Production of bispecific and trispecific F(ab)2 and F(ab)3 antibody derivatives.
R R French
Methods in molecular biology (Clifton, N.J.), 80, 121-134 (1998-07-17)
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.