Characterization and solubilization of cyclo(His-Pro) binding from rat liver membranes.
We have found cyclo(His-Pro) binding in rat liver plasma membranes. This study focused on the characterization of solubilized binding for cyclo(His-Pro) in rat liver membranes. The cyclo(His-Pro) binding of liver membranes was solubilized by digitonin and octyl-glucopyranoside. The efficiency of solubilization with digitonin was greater. However, cyclo(His-Pro) binding was not solubilized by Triton X-100, CHAPS, or Lubrol. Digitonin-solubilized membranes showed cyclo(His-Pro) binding with a high affinity constant (17 nM) and a low binding capacity (38 fmol/mg protein). Lectins from wheat germ, Bandeiraea simplicifolia II, Dolichos biflorus, Glycine max, and Tetragonolobus purpureas significantly adsorbed [3H]cyclo(His-Pro)-binding complex, but Bandeiraea simplicifolia I, Ricinus communis I, or Lens culinaris did not adsorb the binding complex. An analysis of [3H]cyclo(His-Pro)-associated membranes by high performance gel filtration chromatography showed a radioactive peak of Mr 200,000. These data indicate that cyclo(His-Pro) binding of rat liver membranes is solubilized by digitonin and is a glycoprotein of Mr 200,000.[1]References
- Characterization and solubilization of cyclo(His-Pro) binding from rat liver membranes. Mori, M., Yamada, M., Iriuchijima, T., Murakami, M., Kobayashi, S. Proc. Soc. Exp. Biol. Med. (1989) [Pubmed]
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