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Automatic recording apparatus for use in the chromatography of amino acids.
Photometric ninhydrin method for use in the chromatography of amino acids.
In the present investigations of the chromatographic separation of amino acids, it has been observed that, when the color development is carried out in tubes exposed to the air, these difficulties appear to result primarily from the influence of dissolved oxygen. Expand
Chromatography of amino acids on sulfonated polystyrene resins.
A systematic study has been made of the separations of amino acids by elution analysis on columns of synthetic ion exchange resins, demonstrating that synthetic resins are capable of separating most of the common amino acids from one another. Expand
A modified ninhydrin reagent for the photometric determination of amino acids and related compounds.
A modified ninhydrin reagent for the photometric determination of amino acids and related compounds and its application in drug discovery is described. Expand
On the determination of cystine as cysteic acid.
- S. Moore
In the procedure of Schram, Moore, and Bigwood (1) for the determination of the cystine plus cysteine content of a protein, the directions for the concentration of the reaction mixture need to be… Expand
 Chromatographic determination of amino acids by the use of automatic recording equipment
Publisher Summary This chapter describes the chromatographic determination of amino acids by the use of automatic recording equipments. Quantitative determination of amino acids bears a relationship… Expand
The free amino acids of human blood plasma.
It has been possible to identify with a high degree of probability twenty-eight ninhydrin-positive substances in protein-free plasma and to determine most of them quantitatively. Expand
The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins.
On the aggregation of bovine pancreatic ribonuclease.
Effect of divalent cations on the reduction and re-formation of the disulfide bonds of deoxyribonuclease.
These experiments, and the requirement for a divalent cation-DNA complex as the substrate for DNase, demonstrate an ion-protein interaction, and simple gel filtration at neutral pH removes 45Ca++ completely from both the native enzyme and the active form containing only one disulfide bond. Expand