Separation of amino acids, as copper chelates, from amino acid, protein, and peptide mixtures

Fazakerley, S.; Best, Dana

doi:10.1016/0003-2697(65)90093-x

Cited by 64 publications

(9 citation statements)

References 8 publications

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“…The adsorption was run with shaking at room temperature, and lasted 1 h. At the end of the reaction, mixtures were centrifuged (7000g, 10 min), and the supernatants were concentrated in vacuo and lyophilized. The dry residues were washed with diethyl ether three times to remove lypophilic compounds, dissolved in 2 ml of borate buffer (0.05 N solution of sodium tetraborate, pH 11,0), and applied to a column of Sephadex G-25, modified with cupric hydroxide (Fazakerley and Best, 1965). The method allows separation of peptides, as copper chelates, from the mixture of peptides and amino acids.…”

Section: Chemicalsmentioning

confidence: 99%

Detoxication of Phenol in Annual Plant Seedlings

Ugrekhelidze¹,

Kvesitadze²,

Arziani

et al. 1999

Ecotoxicology and Environmental Safety

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Section: Chemicalsmentioning

confidence: 99%

Detoxication of Phenol in Annual Plant Seedlings

Ugrekhelidze¹,

Kvesitadze²,

Arziani

et al. 1999

Ecotoxicology and Environmental Safety

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“…Preliminary experiments showed that ~251-1abeled albumin was taken up by cultured yolk sac and that the products of catabolism were released back into the culture medium. A detailed examination of the hydrolysis products was made, using the Sephadex chromatography methods of Mougey and Mason (19) and Fazakerley and Best (20) as modified by Williams et al (18). Culture media were centrifuged at 2,000 g for 20 min before applying up to 3.0 ml to the columns (40 cm • 1.8 cm diam)…”

Section: Examination Of the Hydrolysis Products Of ~25i-labeled Albuminmentioning

confidence: 99%

Quantitative studies of pinocytosis. II. Kinetics of protein uptake and digestion by rat yolk sac cultured in vitro.

Williams¹,

Kidston²,

Beck³

et al. 1975

The Journal of Cell Biology

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Pinocytic uptake of l~5l-labeled bovine serum albumin by 17.5-day rat visceral yolk sac cultured in vitro has been examined. Uptake was followed by intracellular digestion and, after an initial period, the content of radioactivity in the tissue itself remained constant during the incubation. Radiolabel was returned to the culture medium predominantly as [125I]iodotyrosine; exocytosis of undigested protein did not occur.The rate of uptake of labeled protein, which was constant within an experiment and reproducible between experiments, was much higher than that of a nondigestible macromolecule, l~l-labeled polyvinylpyrrolidone. The higher rate of uptake was a consequence of the protein entering the cells chiefly by adsorption to the plasma membrane being internalized; ~25I-labeled albumin did not stimulate, nor did 125I-labeled polyvinyipyrrolidone inhibit pinocytosis. Different preparations of ~5I-labeled albumin had characteristically different rates of uptake, probably reflecting differences in affinity for plasma membrane receptors. The physiological significance of the findings is discussed.

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“…The problem is of detecting a small amount of peptide in the presence of a large amount of amino acid. A better method is to use the fact that amino acids form complexes with Cu2+ ions, whereas peptides do not (Fazakerley & Best 1965). This gives a very clean separation of the peptide and the free amino acid fractions.…”

Section: Intestinal Infusion Of a Partial Enzymic Hydrolysate Of Casementioning

confidence: 99%