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10dg gel filtration columns  (Bio-Rad)


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    Structured Review

    Bio-Rad 10dg gel filtration columns
    10dg Gel Filtration Columns, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 3896 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/10dg gel filtration columns/product/Bio-Rad
    Average 96 stars, based on 3896 article reviews
    10dg gel filtration columns - by Bioz Stars, 2026-03
    96/100 stars

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    Fig. 8 Solution spectra of protein fraction I (in solid line) and non-protein fraction II (in dashed line) separated by a desalting <t>gel-filtration</t> column (see inset) from the expts listed in Table 3: (a,b) fraction I (a) from expts 1, 2, 4-7 and fraction II (b) from expts 4- 6; (c,d) fraction I (c) and fraction II (d) from expt 3. Absorbance intensity at λ < 450 nm and λ > 450 nm is shown on the left and right vertical axes, respectively. The spectrum (a) is indistinguishable from the spectrum of each purified protein sample alone.
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    Fig. 8 Solution spectra of protein fraction I (in solid line) and non-protein fraction II (in dashed line) separated by a desalting <t>gel-filtration</t> column (see inset) from the expts listed in Table 3: (a,b) fraction I (a) from expts 1, 2, 4-7 and fraction II (b) from expts 4- 6; (c,d) fraction I (c) and fraction II (d) from expt 3. Absorbance intensity at λ < 450 nm and λ > 450 nm is shown on the left and right vertical axes, respectively. The spectrum (a) is indistinguishable from the spectrum of each purified protein sample alone.
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    Fig. 8 Solution spectra of protein fraction I (in solid line) and non-protein fraction II (in dashed line) separated by a desalting gel-filtration column (see inset) from the expts listed in Table 3: (a,b) fraction I (a) from expts 1, 2, 4-7 and fraction II (b) from expts 4- 6; (c,d) fraction I (c) and fraction II (d) from expt 3. Absorbance intensity at λ < 450 nm and λ > 450 nm is shown on the left and right vertical axes, respectively. The spectrum (a) is indistinguishable from the spectrum of each purified protein sample alone.

    Journal: Metallomics : integrated biometal science

    Article Title: Evaluation of Cu(i) binding to the E2 domain of the amyloid precursor protein - a lesson in quantification of metal binding to proteins via ligand competition.

    doi: 10.1039/c7mt00291b

    Figure Lengend Snippet: Fig. 8 Solution spectra of protein fraction I (in solid line) and non-protein fraction II (in dashed line) separated by a desalting gel-filtration column (see inset) from the expts listed in Table 3: (a,b) fraction I (a) from expts 1, 2, 4-7 and fraction II (b) from expts 4- 6; (c,d) fraction I (c) and fraction II (d) from expt 3. Absorbance intensity at λ < 450 nm and λ > 450 nm is shown on the left and right vertical axes, respectively. The spectrum (a) is indistinguishable from the spectrum of each purified protein sample alone.

    Article Snippet: Samples of reaction mixtures (B1.0 mL) were applied to a desalting gel filtration column (Econo-Pac 10DG packed with P6-DG gel, Bio-Rad) equilibrated in Mops buffer (pH 7.4, 100 mM NaCl).

    Techniques: Filtration, Purification