| Literature DB >> 26514871 |
Vicky Ping Chen1, Yang Gao2, Liyi Geng3, Stephen Brimijoin4.
Abstract
A high-throughput radiometric assay was developed to characterize enzymatic hydrolysis of ghrelin and to track the peptide's fate in vivo. The assay is based on solvent partitioning of [(3)H]-octanoic acid liberated from [(3)H]-octanoyl ghrelin during enzymatic hydrolysis. This simple and cost-effective method facilitates kinetic analysis of ghrelin hydrolase activity of native and mutated butyrylcholinesterases or carboxylesterases from multiple species. In addition, the assay's high sensitivity facilitates ready evaluation of ghrelin's pharmacokinetics and tissue distribution in mice after i.v. bolus administration of radiolabeled peptide.Entities:
Keywords: Butyrylcholinesterase; Di-isopropyl fluorophosphates (PubChem CID: 5936); Enzyme kinetics; Ghrelin; Human desacyl-ghrelin (PubChem CID: 71728433); Human ghrelin (PubChem CID: 91668172); Pharmacokinetics; Radiometric assay; Toluene (PubChem CID: 1140); iso-OMPA (PubChem CID: 5420)
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Year: 2015 PMID: 26514871 PMCID: PMC4669970 DOI: 10.1016/j.bcp.2015.10.016
Source DB: PubMed Journal: Biochem Pharmacol ISSN: 0006-2952 Impact factor: 5.858