The Journal of biological chemistry, 262(14), 6856-6863 (1987-05-15)
Unstained frozen hydrated samples of myosin subfragment 1 (S-1) cross-linked to actin with the zero-length cross-linker 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide have been examined by electron microscopy in an effort to probe structural states of the attached cross-bridge. The cross-linked complex in the absence
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
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
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)
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
Il team dei nostri ricercatori vanta grande esperienza in tutte le aree della ricerca quali Life Science, scienza dei materiali, sintesi chimica, cromatografia, discipline analitiche, ecc..
