Chapter 26: Q1TY (page 717)
Find the milliequivalents ofreleased if100mLofwere loaded on a cation exchange column in theform.
Short Answer
The milli equivalents of that will be replaced by 100mL is
Chapter 26: Q1TY (page 717)
Find the milliequivalents ofreleased if100mLofwere loaded on a cation exchange column in theform.
The milli equivalents of that will be replaced by 100mL is
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Get started for freeThe migration time for in a capillary zone electrophoresis experiment is 17.12 min and the migration time for is 17.78 min. From mobilities in Table 15-1, predict the migration time of Br(The observed value is 19.6 min.)
Norepinephrine (NE) in human urine can be assayed by ion-pair chromatography by using an octadecylsilane stationary phase and sodium octyl sulfate as the mobile-phase additive. Electrochemical detection (oxidation at 0.65 V versus Ag|AgCl) is used, with 2,3-dihydroxybenzylamine (DHBA) as internal standard.
Added concentration of NE ( ng/mL ) | Peak height ratio NE/DHBA |
12 | 0.414 |
24 | 0.554 |
36 | 0.664 |
48 | 0.792 |
Electroosmotic velocities of buffered solutions are shown for a bare silica capillary and one with aminopropyl groups (silica—SiOCH2CH2CH2NH2) covalently attached to the wall. A positive sign means that flow is toward the cathode. Explain the signs and relative magnitudes of the velocities.
The water-soluble vitamins niacinamide (a neutral com- pound), riboflavin (a neutral compound), niacin (an anion), and thiamine (a cation) were separated by micellar electrokinetic chromatography in 15mMborate buffer (pH8.0)with 50mMsodium dodecyl sulphate. The migration times were niacinamide (8.1min), riboflavin (13.0min), niacin (14.3min), and thiamine. What would the order have been in the absence of sodium dodecyl sulphate? Which compound is most soluble in the micelles?
Consider a negatively charged protein adsorbed on an anion-exchange gel at pH 8.
(a) How will a gradient of eluent pH (from pH 8to some lower pH) be useful for eluting the protein? Assume that the ionic strength of the eluent is kept constant.
(b) How would a gradient of ionic strength (at constant pH) be useful for eluting the protein?
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