Radiometric assay of ghrelin hydrolase activity and 3H-ghrelin distribution into mouse tissues

Vicky Ping Chen; Yang Gao; Liyi Geng; Stephen Brimijoin

doi:10.1016/j.bcp.2015.10.016

Radiometric assay of ghrelin hydrolase activity and ³H-ghrelin distribution into mouse tissues

Vicky Ping Chen, Yang Gao, Liyi Geng, Stephen Brimijoin

Pharmacology

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

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 [³H]-octanoic acid liberated from [³H]-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.

Original language	English (US)
Pages (from-to)	732-739
Number of pages	8
Journal	Biochemical Pharmacology
Volume	98
Issue number	4
DOIs	https://doi.org/10.1016/j.bcp.2015.10.016
State	Published - Dec 15 2015

Keywords

Butyrylcholinesterase
Enzyme kinetics
Ghrelin
Pharmacokinetics
Radiometric assay

ASJC Scopus subject areas

Biochemistry
Pharmacology

Access to Document

10.1016/j.bcp.2015.10.016

Cite this

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title = "Radiometric assay of ghrelin hydrolase activity and 3H-ghrelin distribution into mouse tissues",

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 [3H]-octanoic acid liberated from [3H]-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.",

keywords = "Butyrylcholinesterase, Enzyme kinetics, Ghrelin, Pharmacokinetics, Radiometric assay",

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T1 - Radiometric assay of ghrelin hydrolase activity and 3H-ghrelin distribution into mouse tissues

AU - Chen, Vicky Ping

AU - Gao, Yang

AU - Geng, Liyi

AU - Brimijoin, Stephen

PY - 2015/12/15

Y1 - 2015/12/15

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AB - 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 [3H]-octanoic acid liberated from [3H]-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.

KW - Butyrylcholinesterase

KW - Enzyme kinetics

KW - Ghrelin

KW - Pharmacokinetics

KW - Radiometric assay

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