000081366 001__ 81366
000081366 005__ 20181203020323.0
000081366 0247_ $$2doi$$a10.1021/ja034145s
000081366 02470 $$2DAR$$a3949
000081366 02470 $$2ISI$$a000183814500030
000081366 037__ $$aARTICLE
000081366 245__ $$aCovalent and selective immobilization of fusion proteins
000081366 269__ $$a2003
000081366 260__ $$c2003
000081366 336__ $$aJournal Articles
000081366 520__ $$aA general method for the covalent immobilization of fusion proteins is presented. The approach is based on the unusual mechanism of the human O6-alkylguanine-DNA alkyltransferase, which irreversibly transfers the alkyl group from its substrate, alkylated or benzylated guanine, to a reactive cysteine residue. By attaching the benzyl group to a surface, hAGT fusion proteins immobilize themselves in a specific and covalent manner. The specificity of the reaction of hAGT with its substrate even allows the specific immobilization of hAGT fusion proteins directly out of cell exts., making the approach an attractive alternative to currently used immobilization procedures. [on SciFinder (R)]
000081366 700__ $$0241538$$aKindermann, Maik$$g148617
000081366 700__ $$0241320$$aGeorge, Nathalie$$g148939
000081366 700__ $$aJohnsson, Nils
000081366 700__ $$0240057$$aJohnsson, Kai$$g123155
000081366 773__ $$j125$$k26$$q7810-7811$$tJournal of the American Chemical Society
000081366 909C0 $$0252027$$pLIP$$xU10102
000081366 909CO $$ooai:infoscience.tind.io:81366$$pSB$$particle
000081366 937__ $$aLIP-ARTICLE-2003-008
000081366 970__ $$a67/LIP
000081366 973__ $$aEPFL$$rREVIEWED$$sPUBLISHED
000081366 980__ $$aARTICLE