• Journal of Ginseng Research
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• v.19 no.3
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• pp.267-274
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• 1995

Vicilin and legumin, the storage Proteins of seed, were Purified from ginseng (Panax ginseng C.A. Meyer) endosperm cells. They were immunized in rabbits, and antibodies were raised respectively. Using these two antibodies, double immunogold labeling of vicilin and legumin was carried out to determine the gap of synthetic time and the transport pattern of vicilin and legumin in the ginseng endosperm cells. Vicilin and legumin were synthesized at the same time at early embryo developmental stage. They were secreted from the Golgi bodies and accumulated into the small vacuoles. As the endosperm cells developed, vicilin and legumin localized in the small vacuoles were gradually transported toward the large central vacuole where they were stored. Protein bodies were derived from the vacuoles filled with proteins and distributed in the endosperm cells of mature red seed. Protein bodies were various in size from 1 to 8 ${\mu}{\textrm}{m}$ in which vicilin and legumin were mixed each other. The number of small particles labeled on the vicilin was greater than that of large particles labeled on the legumin in the protein bodies indicating that the amount of vicilin is higher than that of legumin in the protein bodies.

• Applied Microscopy
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• v.31 no.4
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• pp.347-354
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• 2001

Immunoelectron microscopy of storage protein at early stage of seed development showed legumin was firstly accumulated protein in between endoplasmic reticulum (ER) cisternae, and these accumulates were differentiated into protein body (PB) by transformation at later stage. Thin sections of pea cotyledons during the later stages of seed maturation showed three morphologically different types of protein bodies. One of these, presented as rough-surfaced cisternae with terminal dilations, which contained protein deposits and were often found interdigitated between stacks of rough endoplasmic reticulum. Conventional electron microscopy at earlier stages of cotyledon development showed this protein body type initially developed from the rough ER. This transformation of endoplasmic reticulum into a protein body is believed to represent a new pathway of protein body development.

• Applied Microscopy
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• v.24 no.4
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• pp.86-97
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• 1994

Protein bodies in the endosperm cells of mature red ginseng (Panax ginseng C.A. Meyer) were distributed evenly in the cytoplasm and their size varied from 1 to $8{\mu}m$. Three types of protein bodies were detected and they are spherical or egg-shaped ones containing homogeneous matrix only, spherical ones containing globoids, and irregular shaped ones. Protein bodies degraded in two patterns, one is to start the degration of the body from the surface toward the center, while the other is that the body was broken evenly and then degraded gradually. After degradation, only the limiting membrane remained, that causes the body to be empty. The limiting membranes fused with each other to form a large vacuole. Vicilin and legumin decreased in the endosperm cells as the protein bodies degraded gradually whereas they increased in the umbiliform layers.