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Kang, CC, Chang CC, Cheng JY, Chang TC.  2005.  Simple method in diagnosing cancer cells by a novel fluorescence probe BMVC, Dec. Journal of the Chinese Chemical Society. 52:1069-1072., Number 6 AbstractWebsite

Different cellular accumulations with distinct fluorescence properties of BMVC in cancer cells from normal cells allow us to establish a simple and economic method for the diagnosis of cancer cells. With using a light emitting diode to excite the BMVC molecule, microarray fluorescence analysis of a cell-based glass chip provides an easy method towards the detection of a limited number of cancer cells.

Kang, CC, Chen CT, Cho CC, Lin YC, Chang CC, Chang TC.  2008.  A dual selective antitumor agent and fluorescence probe: the binary BMVC-porphyrin photosensitizer, May. Chemmedchem. 3:725-728., Number 5 AbstractWebsite
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Kang, CC, Chang CC, Chang TC, Liao LJ, Lou PJ, Xie W, Yeung ES.  2007.  A handheld device for potential point-of-care screening of cancer. Analyst. 132:745-749., Number 8 AbstractWebsite

A simple handheld device based on the fluorescence analysis of 3,6-bis(1-methyl-4-vinylpyridinium) carbazole diiodide ( BMVC) stained cells was established for routine screening and potentially for early detection of cancer cells at extremely low cost. Flow cytometry assay further supported the utility of this simple device, where a preliminary study of tissue biopsy showed highly encouraging results.

Kao, WC, Wang VCC, Huang YC, Yu SSF, Chang TC, Chan SI.  2008.  Isolation, purification and characterization of hemerythrin from Methylococcus capsulatus (Bath), Aug. Journal of Inorganic Biochemistry. 102:1607-1614., Number 8 AbstractWebsite

Earlier work from our laboratory has indicated that a hemerythrin-like protein was over-produced together with the particulate methane monooxygenase (pMMO) when Methylococcus capsulatus (Bath) was grown under high copper concentrations. A homologue of hemerythrin had not previously been found in any prokaryote. To confirm its identity as a hemerythrin, we have isolated and purified this protein by ion-exchange, gel-filtration and hydrophobic interaction chromatography, and characterized it by mass spectrometry, UV-visible, CD, EPR and resonance Raman spectroscopy. On the basis of biophysical and multiple sequence alignment analysis, the protein isolated from M. capsulatus (Bath) is in accord with hemerythrins previously reported from higher organisms. Determination of the Fe content in conjunction with molecular-weight estimation and mass analysis indicates that the native hemerythrin in M. capsulatus (Bath) is a monomer with molecular mass 14.8 kDa, in contrast to hemerythrins from other eukaryotic organisms, where they typically exist as a tetramer or higher oligomers. (c) 2008 Elsevier Inc. All rights reserved.