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Purification, identification and preliminary crystallographic studies of an allergenic protein from Lathyrus sativus
A 24 kDa protein was purified from the seeds of Lathyrus sativus by ammonium sulfate fractionation and ion-exchange chromatography. The N-terminal amino-acid sequence showed significant homology with the 2S albumin class of seed storage proteins. The protein showed 85% sequence homology with the see...
Tallennettuna:
| Päätekijät: | , , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
International Union of Crystallography
2006
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2242876/ https://ncbi.nlm.nih.gov/pubmed/16946466 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309106028077 |
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