Clinica chimica acta; international journal of clinical chemistry, 308(1-2), 69-78 (2001-06-20)
Arylesterase (EC 3.1.1.2) activity in serum was specifically measured using thiophenyl acetate in a mechanized assay at 37 degrees C with 4-bromophenylboronic acid as inhibitor of cholinesterase and hexacyanoferrate-III as indicator. The systematic development of a routine method, apparent limitations
Journal of the American Chemical Society, 131(15), 5432-5437 (2009-04-22)
Described herein is the chemical synthesis of the Cys(29)-Gly(77) glycopeptide domain (22) of erythropoietin. Our initial ligation strategy targeted a C --> N termini condensation between glycopeptide 3 and peptide 4. However, the reaction was hindered by the "unattainable" reactivity
Mammalian paraoxonase-1 hydrolyses a very broad spectrum of esters such as certain drugs and xenobiotics. The aim of this study was to determine whether carbamates influence the activity of recombinant PON1 (rePON1). Carbamates were selected having a variety of applications:
The Journal of biological chemistry, 275(43), 33435-33442 (2000-08-10)
The paraoxonase gene family contains at least three members: PON1, PON2, and PON3. The physiological roles of the corresponding gene products are still uncertain. Until recently, only the serum paraoxonase/arylesterase (PON1) had been purified and characterized. Here we report the
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