Membrane-bound heparin binding proteins from HL-60 cells purified in a two-step affinity chromatography differentially eluted with divalent cations

Katsuyuki Imai, Tsukimi Iida, Yasuo Takano, Nobuyuki Uozumi

研究成果: Article査読

3 被引用数 (Scopus)

抄録

Solubilized membrane proteins from HL-60 cells were separated by two-step affinity chromatography. Proteins eluted with MgCl2 in the first heparin-gel were applied to the second heparin-gel and eluted with CaCl2. The eluted proteins were analysed and purified by electrophoresis. N-terminal amino acid sequences of eight proteins on the characteristic bands were determined. Homology search for the sequences indicated that three microsomal proteins, two nuclear proteins and a glycolytic enzyme were eluted with divalent cations, whereas a nuclear ribonucleoprotein and a membrane-cytoskelton linker protein were not dissociated with divalent cations, but with 2 M NaCl. Heparin affinity chromatography combined with differential elution with divalent cations can be a useful method for separation of membrane proteins.

本文言語English
ページ(範囲)1-12
ページ数12
ジャーナルJournal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
780
1
DOI
出版ステータスPublished - 2002 11 15
外部発表はい

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Clinical Biochemistry
  • Cell Biology

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