Isolation and characterization of two types of protein bodies in the rice endosperm
K Tanaka, T Sugimoto, M Ogawa… - Agricultural and …, 1980 - academic.oup.com
K Tanaka, T Sugimoto, M Ogawa, Z Kasai
Agricultural and Biological Chemistry, 1980•academic.oup.comTwo types of proteinaceous particles were observed under the electron microscope in the
starchy endosperm of rice seeds. One was spherical with lamellar structure (PB-I), while the
other was stained homogeneously by osmium tetroxide and not lamellar structured (PB-II).
Both types of proteinaceous particles were effectively condensed from the homogenate of
developing rice endosperm by an aqueous polymer two-phase system using dextran-DEAE
dextran-polyethylene glycol. Separation of both types was carried out by sucrose density …
starchy endosperm of rice seeds. One was spherical with lamellar structure (PB-I), while the
other was stained homogeneously by osmium tetroxide and not lamellar structured (PB-II).
Both types of proteinaceous particles were effectively condensed from the homogenate of
developing rice endosperm by an aqueous polymer two-phase system using dextran-DEAE
dextran-polyethylene glycol. Separation of both types was carried out by sucrose density …
Abstract
Two types of proteinaceous particles were observed under the electron microscope in the starchy endosperm of rice seeds. One was spherical with lamellar structure (PB-I), while the other was stained homogeneously by osmium tetroxide and not lamellar structured (PB-II). Both types of proteinaceous particles were effectively condensed from the homogenate of developing rice endosperm by an aqueous polymer two-phase system using dextran-DEAE dextran-polyethylene glycol. Separation of both types was carried out by sucrose density gradient centrifugation. These proteinaceous particles were recovered at specific gravities of 1.27 and 1.29 for PB-I and PB-II, respectively. The protein composition of these particles and their solubility fractionation were examined. Prolamin appeared in the PB-I fraction, whereas PB-II was rich in glutelin and globulin.
Oxford University Press