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Variability of the Low Molecular Weight Globulin, Conglutin δ, Within Lupin Species
Author(s) -
Species Within Lupin,
Esnault M. A.,
Pichereau V.,
Klingler J.
Publication year - 1997
Publication title -
botanica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.871
H-Index - 87
eISSN - 1438-8677
pISSN - 0932-8629
DOI - 10.1111/j.1438-8677.1997.tb00624.x
Subject(s) - protein subunit , dimer , molecular mass , biochemistry , protein quaternary structure , monomer , storage protein , biology , disulfide bond , polyacrylamide gel electrophoresis , chemistry , enzyme , gene , organic chemistry , polymer
Conglutin δ, a 2S globulin, was purified and compared in six species or varieties of lupin seeds. A common pattern is suggested, present in all species, corresponding to a protein which could exist as a monomer or a dimer. The first form contains one subunit, from 11 to 16.2 kDa, according to the species. It possesses a quaternary structure closely related to conglutin δ1 and was previously described in the narrow‐leaved lupin. The second form contains two similar subunits (23 to 26 kDa) and could be the conglutin δ2. These two subunits are associated even when SDS is used and are probably disulfide‐linked subunits. Each subunit is composed of two disulfide‐linked polypeptides. One is acidic with molecular weight from 14 to 17.3 kDa and the second is acidic to neutral, from 2.4 to 4.5 kDa. Three species ( L. luteus, L. arboreus and L. pilosus ) present a supplementary subunit, with different molecular weight and p than that previously described and which never associates in a dimer form. It has been purified in L. luteus . When native, this protein is oligomeric. The subunit of 12 kDa in this species is composed of a polypeptide of 9 kDa (pl 4.5) disulfide‐linked to one of 3 kDa (pl 6.5). This supplementary protein remains partly associated with the first in the yellow lupin ( L. luteus ). It probably corresponds to a new protein, different from conglutin δ.