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Characterisation of 5'-AMP-activated protein kinase in human liver using specific peptide substrates and the effects of 5'-AMP analogues on enzyme activity.

Abstract：

:A specific peptide (SAMS peptide) phosphorylation assay has previously been used to measure and subsequently purify rat liver 5'-AMP-activated protein kinase (AMPK). In this report, we show that this peptide and a peptide based on the sequence surrounding the site phosphorylated on 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) reductase by AMPK (HMG peptide) can be used to measure human liver AMPK. Our data demonstrate that both human and rat AMPKs have a higher affinity for the HMG peptide compared to the SAMS peptide. We have used these peptide phosphorylation assays to identify novel activators of AMPK.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Sullivan JE,Carey F,Carling D,Beri RK

doi

10.1006/bbrc.1994.1627

subject

Has Abstract

pub_date

1994-05-16 00:00:00

pages

1551-6

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006291X84716275

journal_volume

200

pub_type

杂志文章

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