Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10550060 | Journal of Chromatography B | 2005 | 4 Pages |
Abstract
Membrane proteins were obtained from the mitochondrial fraction of HL-60 cells by solubilization with octyl glucoside and bound to heparin-gels. Bound proteins were successively eluted with solutions containing increasing concentrations of Mg2+ in the first and increasing concentrations of Ca2+ in the second chromatography. After SDS-PAGE and subsequent N-terminal amino acid analysis of proteins on each band, 13 proteins were identified. Fifteen out of the 37 proteins analysed were modified at their N-termini. These results show that this two-step affinity chromatography method using divalent cations as eluents can be applied to a variety of membranes for the isolation of specific proteins.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Tsukimi Iida, Masaharu Kamo, Nobuyuki Uozumi, Takashi Inui, Katsuyuki Imai,