Inhibition of C-terminal O-methyltransferase by a rat liver cytosolic peptide
Archives of Pharmacal Research, ISSN: 0253-6269, Vol: 17, Issue: 5, Page: 354-359
1994
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Article Description
The activity of S-famesylcysteine O-methyltransferase was assayed by incubating the enzyme with a synthetic in vitro substrate, [N-acetyl-S-trans, trans-famesyl-L-cysteine (AFC)], together with S-adenosyl-L-[methyl-C]methionine. The resulting methylesterification product, [N-acetyl-S-trans, trans-famesyl-L-cysteine (methyl-C) ester (AFCME)], was then analyzed either directly on HPLC or by converting the AFC[methyl-C]ME to [methyl-C] alcohol by basehydrolysis. Employing these two analytical methods, it was established that a peptide purified from rat liver cytosol fraction [Int. J. Biochem., 25, 1157 (1993)] strongly inhibited the above enzyme activity with IC of 7.1X10 M. Also, the S-famesylcysteine O-methyltransferase from several human colon cancer cells was also equally inhibited by the peptide. © 1994 The Pharmaceutical Society of Korea.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0028584359&origin=inward; http://dx.doi.org/10.1007/bf02974176; http://link.springer.com/10.1007/BF02974176; http://www.springerlink.com/index/pdf/10.1007/BF02974176; http://link.springer.com/content/pdf/10.1007/BF02974176; http://link.springer.com/content/pdf/10.1007/BF02974176.pdf; http://link.springer.com/article/10.1007/BF02974176/fulltext.html; http://www.springerlink.com/index/10.1007/BF02974176; https://dx.doi.org/10.1007/bf02974176; https://link.springer.com/article/10.1007/BF02974176
Springer Nature
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