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Purification and some properties of an IMP-specific 5'-nucleotidase from yeast.
An IMP-hydrolysing enzyme was purified to homogeneity from yeast extract. It was a soluble protein with an apparent molecular mass of 220 kDa, with a subunit molecular mass of 55 kDa. It was highly specific for IMP, and there was virtually no detectable activity with the other purine and pyrimidine...
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| Huvudupphovsman: | |
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| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
1994
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1137900/ https://ncbi.nlm.nih.gov/pubmed/8141771 |
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