CHARACTERIZATION OF 5'-AMP-ACTIVATED PROTEIN-KINASE IN HUMAN LIVER USING SPECIFIC PEPTIDE-SUBSTRATES AND THE EFFECTS OF 5'-AMP ANALOGS ON ENZYME-ACTIVITY
CHARACTERIZATION OF 5'-AMP-ACTIVATED PROTEIN-KINASE IN HUMAN LIVER USING SPECIFIC PEPTIDE-SUBSTRATES AND THE EFFECTS OF 5'-AMP ANALOGS ON ENZYME-ACTIVITY
复制标题
DOI：
10.1006/bbrc.1994.1627
复制
发表时间：
1994-05-16
影响因子：
3.1
通讯作者：
BERI, RK
中科院分区：
文献类型：
--
作者：
SULLIVAN, JE;CAREY, F;BERI, RK
特异性肽（SAMS肽）磷酸化测定先前已用于测量并随后纯化大鼠肝5 '-AMP-活化蛋白激酶（AMPK）。在这份报告中，我们表明，这种肽和肽的基础上磷酸化的3-羟基-3-甲基戊二酰辅酶A（HMG-CoA）还原酶的AMPK（HMG肽）的网站周围的序列可以用来测量人类肝脏AMPK。我们的数据表明，与SAMS肽相比，人和大鼠AMPK对HMG肽具有更高的亲和力。我们已经使用这些肽磷酸化测定来鉴定AMPK的新激活剂。(C)1994年出版社出版。
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. (C) 1994 Academic Press, Inc.