Reconstitution of Arachin from Isolated Subunits

Yamada, Tetsuo; Aibara, Shigeo; Morita, Yuhei

doi:10.1080/00021369.1981.10864675

Cited by 2 publications

(1 citation statement)

References 5 publications

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“…Yamada et al (1)(2)(3) have shown that arachin consists of six subunits, three of which are acidic and three basic, as revealed by their isoelectric point in a 'monomer' of arachin {9S) component. The models proposed by Pernollett and Mosse (15) and Prakash and Narasinga Rao (11) for the quaternary structure of seed proteins in general fit in very nicely with the arachin molecule.…”

Section: Resultsmentioning

confidence: 99%

Modification of arachin‐effect of citrate ions‐structural implications

Prakash

Rao

1987

J Americ Oil Chem Soc

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The effect of the anion citrate on the subunit structure of arachin has been monitored by velocity sedimentation, viscosity and circular dichroism techniques. The results indicate that as the concentration of citrate ion increases from 25 mM to 150 raM, arachin dissociates progressively to the low molecular weight 2S component. This dissociation is not accompanied by any conformational changes or denaturation as revealed by the far ultraviolet circular dichroic spectra and viscosity results, respectively. The results are explained by direct anion binding and changes in the solvent structure.

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Section: Resultsmentioning

confidence: 99%

Modification of arachin‐effect of citrate ions‐structural implications

Prakash

Rao

1987

J Americ Oil Chem Soc

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Seed storage proteins in coffee

Baú

Mazzafera

Santoro

2001

Rev. Bras. Fisiol. Veg.

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It has been reported that Coffea arabica seeds contain as the main reserve protein, a legumin-like protein, constituted of two subunits, alpha and beta, of approximately 35 and 20 kDa. In this work the seed proteins of several coffee species and varieties were investigated by SDS-PAGE and gel filtration. No differences were observed in the electrophoretic profiles among varieties of C. arabica, however, marked differences were observed among species, or even among individuals of some species. In general, the molecular weight of the subunits alpha and beta accounted for a monomer of 48 to 62 kDa. However, native molecular weight obtained by gel filtration showed that for most of the species there is association of 6 of such proteins, in a hexamer. The most marked difference was observed for C. canephora and C. racemosa. The former clearly showing isoforms of the subunits, and the later showing absence of the beta subunit. The influence of proteases in this observations is discussed.

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Reconstitution of Arachin from Isolated Subunits

Cited by 2 publications

References 5 publications

Modification of arachin‐effect of citrate ions‐structural implications

Modification of arachin‐effect of citrate ions‐structural implications

Seed storage proteins in coffee

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