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- W2013926688 abstract "Plasma membranes from suspension-cultured soybean cells have been enriched with a dextran-polyethylene glycol two-phase system and were used to solubilize the 1,3-β-D-glucan synthase by digitonin. The soluble enzyme bound to spermine which was immobilized on Tresyl-activated Sepharose 4B and could be eluted by about 1 mM spermine ·4 HCl or 40 mM NaCl, indicating a preferential binding to the polyamine. Enzyme activity could be recovered from the column only in the presence of some digitonin. The chromatographed enzyme is still synergistically activated by Ca2+ and polyamines or poly-L-ornithine, indicating a direct and specific interaction with these two types of effectors." @default.
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- W2013926688 date "1987-01-01" @default.
- W2013926688 modified "2023-10-16" @default.
- W2013926688 title "Solubilization, affinity chromatography and Ca2+/polyamine activation of the plasma membrane-located 1,3-β-D-glucan synthase" @default.
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- W2013926688 doi "https://doi.org/10.1016/0168-9452(87)90132-4" @default.
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