Deposition of Matrix and Crystalloid Storage Proteins during Protein Body Development in the Endosperm of Ricinus communis L. cv. Hale Seeds
Author(s) -
David J. Gifford,
John S. Greenwood,
J. Derek Bewley
Publication year - 1982
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.69.6.1471
Subject(s) - endosperm , ricinus , storage protein , polyacrylamide gel electrophoresis , biochemistry , glycoprotein , sudan black b , gel electrophoresis , matrix (chemical analysis) , biology , sodium dodecyl sulfate , vacuole , protein biosynthesis , staining , chemistry , chromatography , gene , genetics , enzyme , cytoplasm
Protein bodies within the endosperm of castor bean (Ricinus communis L. cv. Hale) seeds arise from numerous small vacuoles which progressively become filled with storage protein, of which the crystalloid proteins make up approximately 70%. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) shows that the crystalloids are a family of at least four proteins which reduce to two complementary groups after 2-mercaptoethanol treatment. The matrix, which comprises the remainder, has two major components, the soluble albumins and the lectins. The lectins are the only glycoproteins within the mature protein body. Both cytochemical staining and SDS-PAGE indicate that the synthesis of the crystalloid and the majority of matrix proteins begins some 20 days after pollination. Additionally, the crystalloid proteins are synthesized concurrently, whereas there is temporal variation in the synthesis of matrix proteins.
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