Fast Protein Liquid Chromatography

Abstract Fast protein liquid chromatography (anion exchange) was used to separate glutathione S-transferase isozymes in nontreated etiolated maize shoots and those treated with the herbicide safener CGA -1542814-(dichloroacetyl)-3,4-dihydro-3-methyl-2 H-1 ,4-benzoxazine. Nontreated shoots contained isozymes active with the following substrates: trans-cinnamic acid (1 isozyme), atrazine (3 isozymes), 1-chloro-2,4-dinitrobenzene (1 isozyme), metolachlor (2 isozymes) and the sulfoxide derivative of S-ethyl dipropylcarbamothioate (2 isozymes). Pretreatment of shoots with the safener CGA -154281 (1 μM) had no effect on the activity of the isozymes selective for trans-cinnamic acid and atrazine but increased the activity of the constitutively-expressed isozymes that exhibit activity with 1-chloro-2,4-dinitrobenzene, metolachlor and the sulfoxide derivative of S-ethyl dipropylcarbamothioate. The safener pretreatment also caused the appearance of one new isozyme active with 1-chloro-2,4-dinitrobenzene and one new isozyme active with metolachlor. The results illustrate the complexity of glutathione S-transferase activity in etiolated maize shoots, and the selective enhancement of glutathione S-transferase isozymes by the safener CGA -154281.

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Energy-linked nicotinamide nucleotide transhydrogenase. Properties of proton-translocating mitochondrial transhydrogenase from beef heart purified by fast protein liquid chromatography.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)39776-4 ◽

1984 ◽

Vol 259 (13) ◽

pp. 8626-8632 ◽

Cited By ~ 4

Author(s):

B Persson ◽

K Enander ◽

H L Tang ◽

J Rydström

Keyword(s):

Liquid Chromatography ◽

Fast Protein Liquid Chromatography ◽

Beef Heart ◽

Nicotinamide Nucleotide Transhydrogenase

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Preliminary studies on selenium-containing proteins in Brassica juncea by size exclusion chromatography and fast protein liquid chromatography coupled to ICP-MS

The Analyst ◽

10.1039/b312960h ◽

2004 ◽

Vol 129 (2) ◽

pp. 116 ◽

Cited By ~ 21

Author(s):

Sandra Mounicou ◽

Juris Meija ◽

Joseph Caruso

Keyword(s):

Liquid Chromatography ◽

Brassica Juncea ◽

Size Exclusion Chromatography ◽

Fast Protein Liquid Chromatography ◽

Size Exclusion ◽

Icp Ms ◽

Exclusion Chromatography

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Tryptic phosphopeptides from whole casein. I. Preparation and analysis by fast protein liquid chromatography

Journal of Dairy Research ◽

10.1017/s0022029900029125 ◽

1989 ◽

Vol 56 (4) ◽

pp. 603-611 ◽

Cited By ~ 38

Author(s):

Marcel A. Juillerat ◽

Robert Baechler ◽

Raphael Berrocal ◽

Serge Chanton ◽

Jean-Claude Scherz ◽

...

Keyword(s):

Liquid Chromatography ◽

Anion Exchange ◽

Exchange Resin ◽

Anion Exchange Resin ◽

Gradient Elution ◽

Fast Protein Liquid Chromatography ◽

Parent Species ◽

Net Charge ◽

Phosphorylated Peptides ◽

Salt Gradient

SummaryTryptic phosphopeptides were obtained from whole bovine casein by chromatography on the anion exchange resin QAE-Sephadex A 25. Salt gradient elution of the column allowed separation of non-phosphorylated peptides from phosphorylated species. The preparations obtained contained at least seven distinct phosphopeptides of which the following casein fragments were identified: αs1(43–58):2P, αs1(59–79): 5P, αs2(46–70): 4P, β(1–28): 4P, β(2–28): 4P, and β(33–48): 1P. Fast protein liquid chromatography (FPLC) on Mono Q HR 5/5 resin showed that the phosphopeptides were eluted in the same order as from the QAE-Sephadex resin. However, on the analytical column HR 5/5 the fragments αs1(59–79): 5P and β(2–28): 4P, having the same net charge under the conditions of chromatography, co-eluted, whereas they were at least partly separated on the preparative column HR 16/10. Following enzymic dephosphorylation, the peptides eluted at lower salt strength in the gradient. FPLC on Mono Q resin thus permitted dephosphorylation to be monitored and intermediates between the parent species and the fully dephosphorylated peptide to be identified.

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