Purification and characterization of an oat fructan exohydrolase that preferentially hydrolyzes beta-2,6-fructans.
Oat (Avena sativa cv Fulghum) fructan hydrolase was purified by ammonium sulfate precipitation and anion-exchange, hydrophobic interaction, and size-exclusion chromatography. The enzyme was purified to homogeneity as determined by the presence of a single band (43 kD) on a silver-stained sodium dode...
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| Udgivet i: | Plant Physiol |
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| Principais autores: | , |
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
Oxford University Press
1996
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC157760/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8742337/ https://ncbi.nlm.nih.govhttps://doi.org/10.1104/pp.110.2.639 |
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