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April 27, 2004Socio-Environmental Systems ModelingOpen Access

Characterization of Pea Vicilin. 1. Denoting Convicilin as the α-Subunit of the Pisum Vicilin Family

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FOFrancesca E. O’KaneRHR. P. HappéJVJ.M. Vereijken

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O’Kane et al. (2004) studied this question.

synapsesocial.com/papers/6a8bef34510c7253b5ded9aehttps://doi.org/10.1021/jf035104i
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Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Effects of Glycosylation on Functional Properties of Vicilin, the 7S Storage Globulin from Pea (Pisumsativum)1997 · 38 citations
  2. 2Sequence specificity of the post-translational proteolytic cleavage of vicilin, a seed storage protein of pea (<i>Pisum sativum</i> L.)1983 · 97 citations
  3. 3Immunoaffinity chromatography as a means of purifying legumin from <i>Pisum</i> (pea) seeds1979 · 118 citations
  4. 4The sequence of a gene encoding convicilin from pea (Pisum sativum L.) shows that convicilin differs from vicilin by an insertion near the N-terminus1988 · 63 citations
  5. 5The roles of the N‐linked glycans and extension regions of soybean β‐conglycinin in folding, assembly and structural features1998 · 202 citations