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KMID : 0368419920350020099
Journal of Plant Biology
1992 Volume.35 No. 2 p.99 ~ p.106
Immunocytochemical Localization of Vicilin in Endosperm Cells of Panax ginseng C.A. Meyer
Lee, Chang Seop/ì°óãàð
Yu, Seong Cheol/Kim, Woo Kap/êåà÷ôÉ/ÑÑéÔË£
Abstract
The endosperm protein, vicilin, of ginseng (Panax ginseng C.A. Meyer) was purified by ammonium sulfate precipitaion, gel permeation and ion exchange column chromatography. Vicilin is a glycoprotein composed of 2 subunits with molecular masses of 55,000 (large subunit) and 44,000 (small subunit).
The anti-vicilin antibody was raised in rabbit, and purified by DEAE Affi-Gel Blue affinity chromatography. The endosperm cells of the seed were reacted with this anti-vicilin antibody and colloidal gold conjugated secondary antibody. Gold particles were labelled on the elaborating granules of Golgi complex, electron-dense granules and protein bodies in the endosperm cells.
These results indicated that the vicilin, which was synthesized in rough endoplasmic reticulum and transported to Golgi, was elaborated in saccules of the Golgi and then transported into protein bodies by electron-dense granules.
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