Send to

Choose Destination
See comment in PubMed Commons below
Lab Chip. 2006 Aug;6(8):1056-61. Epub 2006 Jun 19.

Application of a temperature-controllable microreactor to simple and rapid protein identification using MALDI-TOF MS.

Author information

School of Electrical Engineering and Computer Science, Seoul National University, 301-1116, San 56-1, Sillim-Dong, Gwanak-Gu, Seoul 151-742, Korea.


We have carried out a simultaneous thermal denaturation and trypsin digestion of proteins using a temperature-controllable microreactor. This is a simple and rapid sample preparation technique for use before matrix-assisted laser desorption ionization time-of-flight mass spectrometry. In contrast to a conventional sample preparation method, which involves several chemical treatments, our sample preparation was performed using only trypsin digestion with the thermal denaturation of the target protein. Optimization of the reactor operational parameters for trypsin digestion using a temperature-controllable microreactor was carried out. The entire trypsin digestion procedure took about 11 min, and consisted of 1 min for the thermal denaturation of the sample protein (3 microl, 0.2 microM) at 85 degrees C, and 10 min for digestion of the protein at 37 degrees C. The resulting sequence coverage ranged from 24% to 57%, which was sufficient for practical protein identification.

[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Royal Society of Chemistry
    Loading ...
    Support Center