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- W2004893738 abstract "Abstract Further experimental observations support previous circumstantial evidence that binding activity released by osmotic shock functions in the initial step of cyanocobalamin (cyano-B12) transport. A similar specificity for cobalamins (as opposed to cobinamides) was found for the inhibition of cyano-B12[3H] uptake at 37 °, the repression of uptake, the inhibition of cyano-B12[3H] adsorption to whole cells at 0 °, and the inhibition of cyano-B12[3H]-binding to osmotic shock protein at 4 °. In confirmation of these findings, the rate of dicyanocobinamide [3H] uptake at 37 ° was only about 5% of that for cyano-B12[3H]. Osmotic shock, which was shown earlier to reduce 37 ° uptake, also decreased by 3–4-fold the amount of cyano-B12[3H] which whole cells could adsorb at 0 °. Moreover, when cyano-B12[3H] was adsorbed at 0 °, about 80% of it was lost when the washed cells were subsequently shocked. Only 7% was lost, however, if the cells were incubated several minutes at 37 ° to permit transport of the preadsorbed cyano-B12[3H]. Additionally, 0 °-adsorbed cyano-B12[3H] could be removed partially by subjecting whole cells to gel-filtration; whereas, 37 °-transported isotope could not. This and other data strongly indicate that the 0 °-adsorption to whole cells represents the attachment of cyano-B12[3H] to the binders released upon osmotic shock treatment. A cell wall location for the binders and a facilitated-diffusion uptake mechanism are also suggested by the combined data presented here and earlier." @default.
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- W2004893738 date "1972-03-01" @default.
- W2004893738 modified "2023-09-24" @default.
- W2004893738 title "Uptake of cyanocobalamin by Escherichia coli B: Corrinoid specificity and the relationship of a binder" @default.
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- W2004893738 doi "https://doi.org/10.1016/0003-9861(72)90318-9" @default.
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