1956
DOI: 10.1016/0003-9861(56)90255-7
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Protein chromatography on an anion-exchange resin

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Cited by 66 publications
(6 citation statements)
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“…When sulphate or acetate (of equal ionic strength) were substituted for O' 3M chloride ion at pH 8 and 18°C the elution curve of the insulin was very spread. For our purposes the combination of chloride ions and tris buffer cations, which have advantages for chromatography on anion exchange resins (Boman and Westlund 1956) proved the most satisfactory.…”
Section: (B) Effect Of Variation Of Ionic Strength and Nature Of Ionsmentioning
confidence: 91%
“…When sulphate or acetate (of equal ionic strength) were substituted for O' 3M chloride ion at pH 8 and 18°C the elution curve of the insulin was very spread. For our purposes the combination of chloride ions and tris buffer cations, which have advantages for chromatography on anion exchange resins (Boman and Westlund 1956) proved the most satisfactory.…”
Section: (B) Effect Of Variation Of Ionic Strength and Nature Of Ionsmentioning
confidence: 91%
“…introduced which provide new approaches to serum protein separation and characterization (1)(2)(3)(4). Sober, Gutter, Wyckoff, and Peterson, using diethylaminoethyl (DEAE) cellulose, described the initial application of anion-exchange cellulose chromatography to the fractionation and identification of serum proteins (1,2).…”
Section: Chromatographic Techniques Have Recently Beenmentioning
confidence: 99%
“…For another phosphatase, fructose 1:6 diphosphatase, there is evidence that different methods of preparation which allow different degrees of autolysis produce enzymes with different electrophoretic mobilities (Mokrasch & McGilvery, 1956). Other phosphatases which are included among the increasingly large number of proteins that can be resolved by chromatographic or electrophoretic techniques into two or more active components are pancreatic ribonuclease (Martin & Porter, 1951), horse-radish phosphatase (Boman & Westlund, 1956), sweet-potato phosphatase (Ito, Kondo & Watanabe, 1955), rattle-snake-venom phosphodiesterase (Boman & Kaletta, 1956) and yeast phosphomonoesterase (Tsuboi, Wiener & Hudson, 1957). The pea phosphatase has no significant effect on the diester bonds of either diphenyl phosphate or ribonucleic acid, and would therefore probably be classified as a monoesterase.…”
Section: I957mentioning
confidence: 99%