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Ko, Kyong-Cheol,Choi, Mi Hee,Park, Sang Hyun John Wiley Sons, Ltd. 2009 Journal of labelled compounds & radiopharmaceutica Vol.52 No.4
<P>The prototype of the cdc2 protein kinase in mammalian cells regulates its entry into mitosis by phosphorylating a group of key proteins in the major cell cycle transitions. In this study, using the mep45 gene encoding the 45 kDa major envelope protein (Mep45) of Selenomonas ruminantium, a rumen bacteria, a Mep45-fused substrate (PKTPKKAKKL-Mep45, MFS-cdc2) was cloned to detect the activity of cdc2 protein kinase. We report here on a strategy for the detection of a phosphorylation of a substrate catalyzed by cdc2 protein kinase by using a radioisotope detection technique. It is possible to constantly obtain a reasonable quantity of MFS-cdc2 for the cdc2 protein kinase assay and its cost can be as low as a synthesized peptide. Results of the study indicate that the Mep45-fused protein can be used effectively as a substrate for detecting the activity of cdc2 protein kinase and it can be used in developing a protein biochip for a high-throughput screening and also for studying protein–protein interactions. Copyright © 2009 John Wiley & Sons, Ltd.</P> <B>Graphic Abstract</B> <P>Gene cloning and utility phophorylation assay of a protein-fused substrate for a highly sensitive detection of cdc2 protein kinase using a radioisotope detection technique for the development of a protein biochip Kyong-Cheol Ko, Mi Hee Choi, Sang Hyun Park<SUP>*</SUP>Using the mep45 gene encoding the 45 kDa major envelope protein (Mep45) of Selenomonas ruminantium, a rumen bacteria, a Mep45-fused substrate (PKTPKKAKKL-Mep45, MFS-cdc2) was cloned to detect the activity of cdc2 protein kinase. We report here on a strategy for the detection of a phosphorylation of a substrate catalyzed by cdc2 protein kinase by using a radioisotope detection technique. Copyright © 2009 John Wiley & Sons, Ltd. <img src='wiley_img/03624803-2009-52-4-JLCR1579-gra001.gif' alt='wiley_img/03624803-2009-52-4-JLCR1579-gra001'> </P>