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SP sepharose

DEAF Sepharose Fast Flow LC DEAF Sepharose Fast Flow HC DEAF. Spherodex M DEAF. Spherosil M DEAF. Trisacryl Plus M Toyopead DEAE-650 (M) Fractogel EMD DMAE-650 (M) Fractogel EMD DEAE-650 (M) Q Sepharose Fast Flow QMA Spherodex M QMA Spherosil M QMA Trisacryl Plus M Toyopead QAE-550 C SP Sepharose Fast Flow SP Sepharose High Performance SP Sepharose Big Bead SP Trisacryl Plus M Toyopead SP-650 M Fractogel EMD SO -650 M... [Pg.47]

Strong cation Sulfonicacid (SP) NaT HT Li+ 4-13 SP Sepharose SP Sephadex TSKgel SP 5PW... [Pg.43]

Fig. 1. SP Sepharose FF cation exchange chromatography. Fractions collected from a SP Sepharose FF column were resolved in a 15-25% gradient sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) gel and stained with Coomassie blue. Fig. 1. SP Sepharose FF cation exchange chromatography. Fractions collected from a SP Sepharose FF column were resolved in a 15-25% gradient sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) gel and stained with Coomassie blue.
After a further centrifugation step, the supernatant was loaded onto a 25-mL column of SP Sepharose FF (Amersham Biosciences) equilibrated with purification buffer A. [Pg.172]

Figure 1.2 Stained 4—12% SDS-PAGE of expression and purification of HMM protein. Lane 1 is the total soluble fraction from induced and harvested cells, lane 2 is the elution from the Ni-NTA column, and lane 3 is the sample after SP-sepharose purification. An asterisk indicates the HMM protein. Figure is reprinted with permission from Batey and Kieft (2007). Figure 1.2 Stained 4—12% SDS-PAGE of expression and purification of HMM protein. Lane 1 is the total soluble fraction from induced and harvested cells, lane 2 is the elution from the Ni-NTA column, and lane 3 is the sample after SP-sepharose purification. An asterisk indicates the HMM protein. Figure is reprinted with permission from Batey and Kieft (2007).
Fig. 3. Elution profile of the renatured RANTES fusion protein on a Hiload SP Sepharose HR 26/10 column. The protein was eluted with a linear gradient of 0-2 M NaCl as described in Subheading 3.3.1. and 10 mL fractions collected. The result of SDS/PAGE analysis is shown in the insert, showing that the first peak is due to the UV absorbance of glutathione. Fig. 3. Elution profile of the renatured RANTES fusion protein on a Hiload SP Sepharose HR 26/10 column. The protein was eluted with a linear gradient of 0-2 M NaCl as described in Subheading 3.3.1. and 10 mL fractions collected. The result of SDS/PAGE analysis is shown in the insert, showing that the first peak is due to the UV absorbance of glutathione.
Fig. 5. Purification of an incomplete Arg-C digestion of the RANTES fusion. The solution was adjusted to 6 M urea and applied to a Hiload SP Sepharose HR, 26/10 as described in the text. 10 mL fractions were collected. Fig. 5. Purification of an incomplete Arg-C digestion of the RANTES fusion. The solution was adjusted to 6 M urea and applied to a Hiload SP Sepharose HR, 26/10 as described in the text. 10 mL fractions were collected.
The displacer ranking plot has also been employed to compare the affinity of low molecular weight displacers on various classes of ion-exchange materials.54 This study was carried out on three different stationary phases a polymethacrylate (PMA)-based stationary phase (Waters SP-8HR), an agarose-based material (Pharmacia High Performance SP Sepharose), and a hydrophilized PS-DVB support (POROS HS50). These phases are representative of different classes of stationary phases typically employed for protein chromatography. The displacers employed in this study were based on the... [Pg.407]

Bacto Tryptone Bacto Yeast Extract SP-Sepharose fast flow... [Pg.254]

Figure 3.10 Single Component Isotherm of a-Chymotrypsinogen on SP-Sepharose-FF. G. Carta, A. Ubiera, AlCHE ]., 49 (2003) 3066 (Fig. 5). Reproduced by permission of the American Institute of Chemical Engineers. 2003 AIChE. All rights reserved. Figure 3.10 Single Component Isotherm of a-Chymotrypsinogen on SP-Sepharose-FF. G. Carta, A. Ubiera, AlCHE ]., 49 (2003) 3066 (Fig. 5). Reproduced by permission of the American Institute of Chemical Engineers. 2003 AIChE. All rights reserved.
The virus is loaded onto a 5 ml SP Sepharose column (Pharmacia) at a flow rate of 5 ml/min. [Pg.78]

From Pharmacia (Piscataway, NJ) Protein A-Sepharose Fast Flow, Protein G-Sepharose Fast Flow, Sephacryl S-200HR, DEAE-Sepharose CL-4B, Sephadex G-25M, Blue-Sepharose CL-4B, Sephadex G-25 MicroSpin, CM-Sepharose CL-4B, SP-Sepharose Fast Flow. [Pg.2]

This fraction is adjusted to 20 mM potassium phosphate, pH 6.0, by the addition of the appropriate volume of 1 M potassium phosphate, pH 6.0, and chromatographed on a SP-Sepharose column equilibrated with 20 mM phosphate buffer, pH 6.0. [Pg.13]

Apply the sample at a flow rate of 4 ml/min to a 30-mI SP Sepharose Fast Flow column (Pharmacia) equilibrated with buffer A. Wash the column with 10 column volumes of buffer A develop the column with a linear gradient from buffer A to buffer A -I- IM potassium acetate over seven column volumes at a flow rate of 4 ml/min. pfTFB elutes as the major peak centered at 850 mM potassium acetate. [Pg.238]

Fig. 11 Preparative SP-Sepharose high-performance chromatography of a PEGsooo-hGH reaction mixture (panel A). Fractions were pooled as shown on the chromatogram and analyzed by mass spectrometry to determine the average number of PEG5000 groups attached per hGH. Purity for four of the five peaks was further assessed by analytical high-performance liquid chromatography on a sulfopropyl TSK 5PW column (panel B). Reproduced from [69]... Fig. 11 Preparative SP-Sepharose high-performance chromatography of a PEGsooo-hGH reaction mixture (panel A). Fractions were pooled as shown on the chromatogram and analyzed by mass spectrometry to determine the average number of PEG5000 groups attached per hGH. Purity for four of the five peaks was further assessed by analytical high-performance liquid chromatography on a sulfopropyl TSK 5PW column (panel B). Reproduced from [69]...

See other pages where SP sepharose is mentioned: [Pg.355]    [Pg.264]    [Pg.135]    [Pg.305]    [Pg.51]    [Pg.170]    [Pg.11]    [Pg.311]    [Pg.31]    [Pg.43]    [Pg.289]    [Pg.77]    [Pg.409]    [Pg.410]    [Pg.30]    [Pg.1308]    [Pg.87]    [Pg.67]    [Pg.16]    [Pg.138]    [Pg.80]    [Pg.80]    [Pg.80]    [Pg.80]    [Pg.235]    [Pg.1743]    [Pg.531]    [Pg.307]    [Pg.307]    [Pg.245]    [Pg.245]    [Pg.1236]    [Pg.299]   
See also in sourсe #XX -- [ Pg.170 , Pg.172 ]

See also in sourсe #XX -- [ Pg.170 , Pg.172 ]




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Sepharose

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