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4 risultati
Purification, identification and preliminary crystallographic studies of an allergenic protein from Lathyrus sativus.
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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
Crystal structure and functional insights of hemopexin fold protein from grass pea.
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A regulatory protein from grass pea (Lathyrus sativus), LS-24, a close homolog of albumin 2 from garden pea (Pisum sativum) that is associated with polyamine biosynthesis, was characterized and the structure of a hemopexin-type fold among plant proteins illustrated. Crystal structure of LS-24
Storage proteins from Lathyrus sativus seeds.
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The proteins from Lathyrus sativus Linn. (chickling vetch or grass pea) seeds were investigated. Protein constitutes approximately 20% of the seed dry weight, >60% of which is composed by globulins and 30% by albumins. A single, 24 kDa polypeptide comprises more than half of the protein present in
Localisation of amino acid sequence stretches containing a continuous epitope on the surface of the two Lathyrus ochrus isolectins.
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A series of 66 overlapping heptapeptides covering the complete amino acid sequences of the heavy subunits (beta chains) of the two Lathyrus ochrus isolectins (LoLI and LoLII) were synthesised and coupled to bovine serum albumin used as a carrier protein, and the conjugates were allowed to react with
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