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Literature DB >> 849259

Biospecific-elution chromatography with 'imphilytes' as stationary phases.

Abstract

Six out of seven enzymes tested (four of them nicotinamide nucleotide-dependent dehydrogenases) showed differences in chromatographic behaviour in the presence and absence of their biospecific ligands, when chromatographed on immobilized amphipathic ampholytes ('imphilytes') as stationary phases. Some enzymes were adsorbed more tightly, others less tightly, in the presence of ligands. These results have implications for enzyme purification in general, and for some types of affinity chromatography in particular.

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Year: 1977 PMID： 849259 PMCID： PMC1164500 DOI： 10.1042/bj1610233

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

12 in total

1. Protein chromatography on adsorbents with hydrophobic and ionic groups. Some properties of N-(3-carboxypropionyl)aminodecyl-sepharose and its interaction with wheat-germ aspartate transcarbamoylase.

Authors: R J Yon; R J Simmonds
Journal: Biochem J Date: 1975-11 Impact factor: 3.857

2. Protein chromatography on adsorbents with hydrophobic and ionic groups. Chromatography of dodecyl sulphate-solubilized proteins of the human erythrocyte membrane on N-(3-carboxypropionyl)aminodecyl-sepharose.

Authors: R J Simmonds; R J Yon
Journal: Biochem J Date: 1976-07-01 Impact factor: 3.857

6. Enzyme purification by hydrophobic chromatography: an alternative approach illustrated in the purification of aspartate transcarbamoylase from wheat germ.

Authors: R J Yon
Journal: Biochem J Date: 1974-01 Impact factor: 3.857

10. Affinity chromatography of nicotinamide-adenine dinucleotide-linked dehydrogenases on immobilized derivatives of the dinucleotide.

Authors: S Barry; P O'Carra
Journal: Biochem J Date: 1973-12 Impact factor: 3.857

3 in total

1. The adsorption of proteins and protein--dodecyl sulphate complexes on N-(3-carboxypropionyl)aminodecyl-Sepharose.

Authors: R J Yon; R J Simmonds
Journal: Biochem J Date: 1979-02-01 Impact factor: 3.857

2. Sensitivity and other factors affecting biospecific desorption in chromatography of proteins. A study by computer simulation.

Authors: R J Yon
Journal: Biochem J Date: 1980-01-01 Impact factor: 3.857

3. Wheat-germ aspartate transcarbamoylase. Purification and cold-lability.

Authors: J E Grayson; R J Yon; P J Butterworth
Journal: Biochem J Date: 1979-11-01 Impact factor: 3.857

3 in total

Biospecific-elution chromatography with 'imphilytes' as stationary phases.

1. Protein chromatography on adsorbents with hydrophobic and ionic groups. Some properties of N-(3-carboxypropionyl)aminodecyl-sepharose and its interaction with wheat-germ aspartate transcarbamoylase.

2. Protein chromatography on adsorbents with hydrophobic and ionic groups. Chromatography of dodecyl sulphate-solubilized proteins of the human erythrocyte membrane on N-(3-carboxypropionyl)aminodecyl-sepharose.

3. Affinity chromatography of kinases and dehydrogenases on Sephadex and Sepharose dye derivatives.

4. Interfering and complicating adsorption effects in bioaffinity chromatography.

5. Affinity elution: principles and applications to purification of aminoacyl-tRNA synthetases.

6. Enzyme purification by hydrophobic chromatography: an alternative approach illustrated in the purification of aspartate transcarbamoylase from wheat germ.

7. Chromatography of lipophilic proteins on adsorbents containing mixed hydrophobic and ionic groups.

8. Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. I. Isolation and subunit structure.

9. Wheat-germ aspartate transcarbamoylase. Kinetic behaviour suggesting an allosteric mechanism of regulation.

10. Affinity chromatography of nicotinamide-adenine dinucleotide-linked dehydrogenases on immobilized derivatives of the dinucleotide.

1. The adsorption of proteins and protein--dodecyl sulphate complexes on N-(3-carboxypropionyl)aminodecyl-Sepharose.

2. Sensitivity and other factors affecting biospecific desorption in chromatography of proteins. A study by computer simulation.

3. Wheat-germ aspartate transcarbamoylase. Purification and cold-lability.