DNA-maleimide: an improved maleimide compound for electrophoresis-based titration of reactive thiols in a specific protein.

Satoshi Hara, Tatsuya Nojima, Kohji Seio, Masasuke Yoshida, Toru Hisabori

Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta 4259-R1-8, Midori-ku, Yokohama 226-8503, Japan.

Biochimica et biophysica acta 2013 Apr

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Thiol-mediated redox regulation of proteins plays a key role in many cellular processes. To understand the redox status of cysteinyl thiol groups of the desired proteins, we developed a new maleimide reagent: a maleimide-conjugated single strand DNA, DNA-maleimide (DNA-Mal). DNA-Mal labelled proteins run as a distinct band on SDS-PAGE, with a discrete 9.32 kDa mobility shift per label regardless of the protein species or electrophoretic conditions. DNA-Mal labels free thiols like standard maleimide reagents, but possesses practical advantages in titration of the number and relative content of free thiols in a protein. The versatility of DNA molecule enhances the application of DNA-Mal in a broader range of cysteine containing proteins. Copyright © 2013 Elsevier B.V. All rights reserved.

Citation

Satoshi Hara, Tatsuya Nojima, Kohji Seio, Masasuke Yoshida, Toru Hisabori. DNA-maleimide: an improved maleimide compound for electrophoresis-based titration of reactive thiols in a specific protein. Biochimica et biophysica acta. 2013 Apr;1830(4):3077-81