Electron microscopic observation of thin sections of rice (Oryza safiva L.) endosperm revealed two types of protein bodies (PBs): spherical and irregular-shaped ones. lmmunocytochemical localization studies using antibodies raised against purified glutelins, prolamines, and globulins indicated that the prolamines were localized in the spherical PB, whereas the irregular-shaped PB contained glutelins and globulins. We counted and measured the surface area and the relative volume of 2303 PBs randomly selected from two different developmental stages and from different locations within the endosperm. The ratio of spherical to irregular-shaped PBs was 1 :1.6. Double-label immunogold electron microscopic localization indicated that the globulins represented about 18% of the surface area of the irregular-shaped PBs. Based on our morphometric analysis, we estimate the relative contribution of glutelin as 53%, that of prolamine as 35%, and that of globulin as 12% of the total seed protein.Seed storage proteins can be divided into four classes based on their solubility properties. Albumins are water soluble, globulins are salt soluble, prolamines are soluble in aqueous alcohol solutions, and glutelins are soluble in alkali or acid (Shotwell and Larkins, 1989). Rice (Oryza sativa L.), a staple food crop for millions of people worldwide, has a seed protein content ranging from 5 to 12% (Villareal and Juliano, 1978). The major storage proteins found in rice are the glutelins, which according to previous studies, account for 80% or more of the total seed protein (Tecson et al., 1971;Juliano, 1972;Villareal and Juliano, 1978). The remaining 20% is divided as follows: albumins, 1 to 5%; globulins, 4 to 15%; and prolamines, 2 to 8% (Houston et al., 1968). It has been demonstrated that the relative contributions of each of the solubility classes of seed proteins can be influenced by genotype, growing conditions, and the analytical methods employed (Sugimoto et al., 1986;Ogawa et al., 1987;Huebner et al., 1990).The biosynthesis of rice glutelins and prolamines has been studied in detail by severa1 researchers (Yamagata et , 1982;Luthe, 1983;Wen and Luthe, 1985;Li and Okita, 1993). Glutelins are first synthesized as precursor proteins of 51 to 57 kD. These precursors are then proteolytically processed into a subunits of 34 to 39 kD and fl subunits of 21 to 22 kD. The end products are stored in specialized structures called PBs. A previous electron microscopic study found that glutelins are processed through the Golgi apparatus and are deposited in irregular-shaped PBs (PB type I). Rice prolamines have molecular masses in the 10-to 17-kD range (Mandac and Juliano, 1978;Kim and Okita, 1988;Masumura et al., 1990) and accumulate within distensions of the rough ER (Yamagata et al., 1982;. They are stored in spherical PBs (PB type 11). Recently, the relative contribution of prolamines to the total protein content of rice seeds has been re-examined. Traditionally, prolamines have been extracted with 70% ethanol. However, a study by Sugi...