A "Batch" microcalorimeter is used at 30 degrees C for the study of the hydrolysis of 4-nitro-phenylphenylphosphonate with a calf-intestinal phosphonate esterase, in a tris buffer, pH 8. The yield of enzymatic hydrolysis is estimated by spectrophotometric determination of the
A bifunctional activity label (8) for directed molecular evolution of lipolytic enzymes has been designed and synthesized. The structure is composed of a 4-nitrophenyl activated phosphonate, that is, a suicide substrate of lipases/esterases, connected to a biotin moiety through a
Hydrolysis of a phosphonate ester catalyzed by an enzyme from Dictyostelium discoideum.
E F Rossomando et al.
Archives of biochemistry and biophysics, 197(1), 364-366 (1979-10-01)
Several laboratories have now shown that monoclonal antibodies having enzyme-like properties can be generated. The generation of catalytic antibodies makes use of the same basic procedures that have been used for the generation of binding monoclonal antibodies, yet the process
To determine the cerebral metabolism of patients with cortical visual loss. Two observational case studies. Two patients who survived acute organophosphate poisoning with respiratory failure experienced severe visual loss despite relatively normal ophthalmic examination results. Magnetic resonance imaging of the
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