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. 1969 Apr;44(4):471–479. doi: 10.1104/pp.44.4.471

Immunochemical Studies on Arachis hypogaea Proteins With Particular Reference to the Reserve Proteins. I. Characterization, Distribution, and Properties of α-Arachin and α-Conarachin 1

J Daussant a,2, N J Neucere a,3, L Y Yatsu a,3
PMCID: PMC396112  PMID: 16657087

Abstract

Fourteen antigenic constituents have been detected in Arachis hypogaea seeds. The major proteins of the classic arachin and conarachin fractions have been identified. Arachin contains 4 antigens (the major one called α-arachin) and conarachin contains 2 which have been called α1, and α2-conarachin. Structural differences between α-arachin, α1 and α2-conarachin are indicated by their different antigenic specificities. α-Arachin precipitates as a separate entity at low temperature. The action of trypsin on this protein induces an increase in electrophoretic mobility and prevents precipitation at low temperature. This enzyme has no detectable effect on α1 and α2-conarachin.

The proteins of the cotyledon and of the entire axis are quite similar in their immunoelectrophoretic patterns. However, quantitative and qualitative differences occur between the proteins found in the cotyledon and those of the 1-millimeter tip of the axis. In the latter, there is a 4-fold smaller proportion of α-arachin than in the cotyledon. Immunoelectrophoretic analysis of subcellular preparations from cotyledons confirms that α-arachin is an aleurin and that α1-conarachin is a typical cytoplasmic protein. Large and small aleurone grains appear very similar in their qualitative antigenic composition.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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