Cereal Chem 67:360-366 | VIEW
Immunocytochemical Evidence for the Involvement of the Golgi Apparatus in the Transport of the Vacuolar Protein, Gamma-Secalin, in Rye (Secale cereale) Endosperm.
H. B. Krishnan, J. A. White, and S. T. Pueppke. Copyright 1990 by the American Association of Cereal Chemists, Inc.
We resolved the alcohol-soluble prolamins of rye endosperm (secalins) by sodium dodecyl sulfate- polyacrylamide gel electrophoresis into four groups of proteins: high molecular weight (HMW) secalins, 68,000- and 57,000-dalton gamma-seclins, omega-secalins, and 33,000-dalton gamma-secalins. Antibodies raised against wheat prolamins reacted specifically with gamma-secalins of rye upon protein blot analysis. Thin sections of rye grains were examined immunocytochemically with these antibodies. Gamma-secalins were present primarily in protein bodies. Vesicles arising from the Golgi apparatus also were specifically labeled, whereas the cytosol and other organelles, including mitochondria, lipid bodies, and amyloplasts, were not. These observations support the hypothesis that the transport of gamma-secalins from the site of synthesis (rough endoplasmic reticulum) to that of deposition (protein bodies) is mediated by the Golgi apparatus in rye caryopses.