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Elution pattern from cellulose column

Figure 3. Typical elution patterns (from carboxymethyl cellulose columns) of intramuscular connective tissue extracted from beef semitendinosus muscle. A. (above) unaged B. (below) 13 days postmortem (33). Figure 3. Typical elution patterns (from carboxymethyl cellulose columns) of intramuscular connective tissue extracted from beef semitendinosus muscle. A. (above) unaged B. (below) 13 days postmortem (33).
Fig. 1. Elution pattern of human plasma cholinesterase from DEAE-cellulose column solid line, absorbance at 280 nm broken line, enzyme activity. Partially purified enzyme preparation was placed on a DEAE-cellulose column (1.2 x 10 cm) and equilibrated with 0.02 mol/liter acetate buffer, pH 6.0. The column was washed with the same buffer containing 0.06 mmol/liter sodium chloride (up to 400 ml of effluent). Then (at single arrow) the enzyme was eluted with a linear gradient of sodium chloride and choline chloride ranging in concentration from 0.06 mmol/liter NaCl to 0.03 mmol/liter NaCl + 0.03 mol/liter choline chloride. At the double arrow, the buffer was changed to 0.02 mol/liter acetate buffer, pH 6.0, containing 0.2 mol/liter NaCl flow rate 25 ml per hour. (After Yoshida, Y2.)... Fig. 1. Elution pattern of human plasma cholinesterase from DEAE-cellulose column solid line, absorbance at 280 nm broken line, enzyme activity. Partially purified enzyme preparation was placed on a DEAE-cellulose column (1.2 x 10 cm) and equilibrated with 0.02 mol/liter acetate buffer, pH 6.0. The column was washed with the same buffer containing 0.06 mmol/liter sodium chloride (up to 400 ml of effluent). Then (at single arrow) the enzyme was eluted with a linear gradient of sodium chloride and choline chloride ranging in concentration from 0.06 mmol/liter NaCl to 0.03 mmol/liter NaCl + 0.03 mol/liter choline chloride. At the double arrow, the buffer was changed to 0.02 mol/liter acetate buffer, pH 6.0, containing 0.2 mol/liter NaCl flow rate 25 ml per hour. (After Yoshida, Y2.)...
Figure 3. Elution pattern for the cyclic dextrins from a cellulose column by a solvent mixture of water, ethanol and 1-butanol of the composition indicated on the chart and at a temperature of 75°C. (Reproduced with permission from Ref. 11. Copyright 1961 Academic Press.)... Figure 3. Elution pattern for the cyclic dextrins from a cellulose column by a solvent mixture of water, ethanol and 1-butanol of the composition indicated on the chart and at a temperature of 75°C. (Reproduced with permission from Ref. 11. Copyright 1961 Academic Press.)...
Figure 2. Chromatographic elution pattern of mouse sub-maxillary gland renin at its final purification step from a carboxymethyl cellulose column at pH 5.4. Renin activity (-0-) was determined by the method of Reinharz and Roth (62), Protein concentration (—A--) was measured by absorbance at 280 nm. Ref. (54). Figure 2. Chromatographic elution pattern of mouse sub-maxillary gland renin at its final purification step from a carboxymethyl cellulose column at pH 5.4. Renin activity (-0-) was determined by the method of Reinharz and Roth (62), Protein concentration (—A--) was measured by absorbance at 280 nm. Ref. (54).
Fig 2-Elution profile from a DEAE cellulose column(cm 2 X 30).Elution buffer 10 mM Tris-Cl,pH 8 500 mg proteins. Specific activity= 4moles " C02/hr/g. Insert=chromatographic pattern of active fraction on cellulose thin layer developped in butanol-pyridine -acetic acid-water(45 30 9 36)and sprayed with ninhydrin. [Pg.348]

Figure 19. A Gel filtration pattern of a 40X1 tryptic hydrolysate (1 hr) of bovine serum albumin. The hydrolysate (0.3 g) was applied onto a column (2.7 x 80 cm) of Sephadex G-100 which was eluted with 0.01 M NH HCOs. Fractions (7.5 ml each) were analyzed continuously by an ultraviolet monkor. B Chromatogi hic pattern on DEAE-cellulose of peak 3 from A. The material (100 mg) was applied on a column (1.5 x 20 cm) which was subjected to stepwise elution. Initial elution was with 0.005 M sodium phosphate buffer at pH 6.2. At positioa 2 the column was eluted with 0.0175 M phosphate buffer pH 6.2, and at portion 3 the ehient was changed to 0.0175 M phosphate pH 6.2 plus 0.077 M NaCl. Fractions (3 ml) were read continuously by an ultraviolet monitor. From Habeeb and Atassi (19766). Figure 19. A Gel filtration pattern of a 40X1 tryptic hydrolysate (1 hr) of bovine serum albumin. The hydrolysate (0.3 g) was applied onto a column (2.7 x 80 cm) of Sephadex G-100 which was eluted with 0.01 M NH HCOs. Fractions (7.5 ml each) were analyzed continuously by an ultraviolet monkor. B Chromatogi hic pattern on DEAE-cellulose of peak 3 from A. The material (100 mg) was applied on a column (1.5 x 20 cm) which was subjected to stepwise elution. Initial elution was with 0.005 M sodium phosphate buffer at pH 6.2. At positioa 2 the column was eluted with 0.0175 M phosphate buffer pH 6.2, and at portion 3 the ehient was changed to 0.0175 M phosphate pH 6.2 plus 0.077 M NaCl. Fractions (3 ml) were read continuously by an ultraviolet monitor. From Habeeb and Atassi (19766).

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Elution column

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