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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...

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Bibliografski detalji
Glavni autori: Qureshi, Insaf A., Sethi, Dhruv K., Salunke, Dinakar M.
Format: Artigo
Jezik:Inglês
Izdano: International Union of Crystallography 2006
Teme:
Online pristup: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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