Measurement of protein by spectrophotometry at 205 nm

Scopes, Robert K.

doi:10.1016/0003-2697(74)90034-7

Cited by 729 publications

(453 citation statements)

References 11 publications

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“…The A280 of a 1-mg/ml solution of the pure enzyme is 1.28, based on protein determination by the 205/280-nm method (23).…”

Section: Resultsmentioning

confidence: 99%

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Pyruvate decarboxylase of Zymomonas mobilis: isolation, properties, and genetic expression in Escherichia coli

Neale¹,

Scopes²,

Wettenhall³

et al. 1987

J Bacteriol

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Pyruvate decarboxylase (EC 4.1.1.1) from Zymomonas mobilis purified to homogeneity by using dye-ligand and ion-exchange chromatography. Antibodies produced against the enzyme and the amino-terminal sequence obtained for the pure enzyme were used to select and confirm the identity of a genomic clone encoding the enzyme selected from a genomic library of Z. mobilis DNA cloned into pUC9. The genomic fragment encoding the enzyme expressed high levels of pyruvate decarboxylase in Escherichia coli. Possible RNA polymerase and ribosome-binding sites have been identified in the 5'-untranslated region of the pyruvate decarboxylase gene.

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“…The A280 of a 1-mg/ml solution of the pure enzyme is 1.28, based on protein determination by the 205/280-nm method (23).…”

Section: Resultsmentioning

confidence: 99%

“…Activity is expressed in micromoles per minute at 25°C. Protein was measured by the dye-binding method (27), and the pure enzyme was quantitated by measuring A205,280 (23).…”

Section: Methodsmentioning

confidence: 99%

Pyruvate decarboxylase of Zymomonas mobilis: isolation, properties, and genetic expression in Escherichia coli

Neale¹,

Scopes²,

Wettenhall³

et al. 1987

J Bacteriol

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“…However, the Edelhoch method is convenient and accurate, and the best approach is still to measure rather than predict t . If you are unlucky and have a protein with no Trp or Tyr, the paper by Scopes (1974) should be consulted.…”

Section: Predicting the Absorption Coefficient Of A Proteinmentioning

confidence: 99%

How to measure and predict the molar absorption coefficient of a protein

et al. 1995

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The molar absorption coefficient, E, of a protein is usually based on concentrations measured by dry weight, nitrogen, or amino acid analysis. The studies reported here suggest that the Edelhoch method is the best method for measuring E for a protein. (This method is described by Gill and von Hippel [1989, Anal Biochem 182:319-3261 and is based on data from Edelhoch [ , Biochemistry 6:1948.) The absorbance of a protein at 280 nm depends on the content of Trp, Tyr, and cystine (disulfide bonds). The average E values for these chromophores in a sample of 18 well-characterized proteins have been estimated, and the E values in water, propanol, These ~(280) values are quite reliable for proteins containing Trp residues, and less reliable for proteins that do not. However, the Edelhoch method is convenient and accurate, and the best approach is to measure rather than predict E .

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“…Proteins were quantified either by the method of Bradford [23] for crude extracts with bovine c-globulin as standard or, for pure proteins, by measuring A 205nm [24]. Pure enzyme concentration is expressed on a monomer basis (45 kDa).…”

Section: Protein Quantificationmentioning

confidence: 99%

Identification of a plant gene encoding glutamate/aspartate‐prephenate aminotransferase: The last homeless enzyme of aromatic amino acids biosynthesis

et al. 2010

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Edited by Ulf-Ingo Flügge Keywords:Aspartate aminotransferase Aromatic amino acid Enzymology Metabolism Plant Prephenate aminotransferase a b s t r a c tIn all organisms synthesising phenylalanine and/or tyrosine via arogenate, a prephenate aminotransferase is required for the transamination of prephenate into arogenate. The identity of the gene encoding this enzyme in the organisms where this activity occurs is still unknown. Glutamate/aspartate-prephenate aminotransferase (PAT) is thus the last homeless enzyme in the aromatic amino acids pathway. We report on the purification, mass spectrometry identification and biochemical characterization of Arabidopsis thaliana prephenate aminotransferase. Our data revealed that this activity is housed by the prokaryotic-type plastidic aspartate aminotransferase (At2g22250). This represents the first identification of a gene encoding PAT.

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Measurement of protein by spectrophotometry at 205 nm

Cited by 729 publications

References 11 publications

Pyruvate decarboxylase of Zymomonas mobilis: isolation, properties, and genetic expression in Escherichia coli

Pyruvate decarboxylase of Zymomonas mobilis: isolation, properties, and genetic expression in Escherichia coli

How to measure and predict the molar absorption coefficient of a protein

Identification of a plant gene encoding glutamate/aspartate‐prephenate aminotransferase: The last homeless enzyme of aromatic amino acids biosynthesis

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