Purification and properties of glutamate dehydrogenase from a thermophilic bacillus.
A 250- to 300-fold purification of a nicotinamide adenine denucleotide phosphate (NADP)-dependent glutamate dehydrogenase (GDH, E.C. 1.4.1.4) with a yield of 60% from a thermophilic bacillus is described. More than one NADP-specific GDH was detected by polyacrylamide gel electrophoresis. The enzyme...
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| Vydáno v: | J Bacteriol |
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| Hlavní autoři: | , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Microbiology (ASM)
1975
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC246183/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/238942/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.122.3.1257-1264.1975 |
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