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Glutamate dehydrogenase from bovine liver

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Glutamate dehydrogenase from bovine liver is an enzyme that catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia. It is an important enzyme in the metabolism of amino acids and nitrogen.

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Lab products found in correlation

Yeast alcohol dehydrogenase, by Merck Group (2 mentions) Glycogen phosphorylase b from rabbit muscle, by Merck Group (2 mentions) Rabbit aldolase, by Merck Group (2 mentions) Horse liver alcohol dehydrogenase, by Merck Group (2 mentions) Pyruvate kinase, by Merck Group (2 mentions) Beta galactosidase from escherichia coli, by Merck Group (2 mentions) Groes, by Merck Group (2 mentions)

2 protocols using glutamate dehydrogenase from bovine liver

1

Preparation of Protein Complexes

Check if the same lab product or an alternative is used in the 5 most similar protocols
Protein complex samples, including glycogen phosphorylase b from rabbit muscle (195 kDa), glutamate dehydrogenase from bovine liver (334 kDa), beta-galactosidase from Escherichia coli (464 kDa), horse liver alcohol dehydrogenase (80 kDa), yeast alcohol dehydrogenase (147 kDa), rabbit aldolase (158 kDa), GroES (84 kDa), and pyruvate kinase (232 kDa) were purchased from Sigma-Aldrich (St. Louis, MO). GroEL from Escherichia coli (802 kDa) was prepared57 and provided by Dr. I.D.G.C.; human superoxide dismutase (32 kDa) was provided by Dr. Y. Sheng and human transferrin receptor (157 kDa) was provided by Dr. M. Penichet.
Li H., Nguyen H.H., Ogorzalek Loo R.R., Campuzano I.D, & Loo J.A. (2018). An Integrated Native Mass Spectrometry and Top-Down Proteomics Method that Connects Sequence to Structure and Function of Macromolecular Complexes. Nature chemistry, 10(2), 139-148.
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2

Preparation of Protein Complexes

Check if the same lab product or an alternative is used in the 5 most similar protocols
Protein complex samples, including glycogen phosphorylase b from rabbit muscle (195 kDa), glutamate dehydrogenase from bovine liver (334 kDa), beta-galactosidase from Escherichia coli (464 kDa), horse liver alcohol dehydrogenase (80 kDa), yeast alcohol dehydrogenase (147 kDa), rabbit aldolase (158 kDa), GroES (84 kDa), and pyruvate kinase (232 kDa) were purchased from Sigma-Aldrich (St. Louis, MO). GroEL from Escherichia coli (802 kDa) was prepared57 and provided by Dr. I.D.G.C.; human superoxide dismutase (32 kDa) was provided by Dr. Y. Sheng and human transferrin receptor (157 kDa) was provided by Dr. M. Penichet.
Li H., Nguyen H.H., Ogorzalek Loo R.R., Campuzano I.D, & Loo J.A. (2018). An Integrated Native Mass Spectrometry and Top-Down Proteomics Method that Connects Sequence to Structure and Function of Macromolecular Complexes. Nature chemistry, 10(2), 139-148.
+ Open protocol
+ Expand

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