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)
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
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
The Journal of biological chemistry, 258(11), 6941-6946 (1983-06-10)
Extensive kinetic studies of bovine intestinal 5'-nucleotide phosphodiesterase as a function of pH have confirmed and amplified the catalytic mechanism previously proposed on the basis of isolation of a covalent phosphorylated intermediate (Landt, M., and Butler, L.G. (1978) Biochemistry 17
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