期刊
PROTEIN EXPRESSION AND PURIFICATION
卷 31, 期 1, 页码 161-165出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/S1046-5928(03)00144-X
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Metallothioneins (NIT) are small cysteine-rich proteins, expressed in many life forms. They are involved primarily in the metabolism of zinc and copper, and in metal detoxification processes. Metallothionein-3 is a mammalian brain-specific NIT, which is down-regulated in Alzheimer's disease brains. In this report, we describe a new procedure for purification of recombinant human apo-MT-3 by three steps, size exclusion at neutral pH, followed by cation-exchange and reverse-phase HPLC, both at low pH. Purified apo-MT-3 was reconstituted with seven Zn2+ ions and reconstitution products were analyzed with electrospray ionization mass spectrometry. The mass spectrum of reconstituted ZnMT-3 was identical with that of native ZnMT-3 isolated by size exclusion chromatography proving the efficiency of the reconstitution process. It showed that ZnMT-3 exists in solution as a dynamic mixture of several metalloforms, where the main metalloform is Zn7MT-3 and minor forms are Zn6MT-3 and Zn8MT-3. (C) 2003 Elsevier Science (USA). All rights reserved.
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