• Applied Microscopy
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• 제14권2호
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• pp.15-28
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• 1984

The endosperm cells and the umbiliform layer of ginseng (Panax ginseng C.A. Meyer) seed are studied with light and electron microscope. Differentiated mitochondria, ER cisternae, proplastids and ribosomes are characteristically observed in the endosperm cells of matured seed. The cell inclusions contain the protein bodies and the spherosomes. Protein body contains, in proteinaceous matrix, globoids and crystalloids. Particularly the crystalloids have the lattice structure, and the formation of globoids is closely related with ER. Umbiliform layer has the positive reaction on alcian blue (pH 2.5) and the metachromasis on the toluidine blue. The umbiliform layer is formed by autolysis of endosperm cells, and composed of the deformated cell wall and the lipoprotein bodies. Particularly a part of the lipoprotein body and the fibrilar network structure have the positive reaction on acid phosphatase.

• Preventive Nutrition and Food Science
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• 제6권1호
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• pp.29-37
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• 2001

The mobilization of food reserves and ultrastructural changes in th cotyledons of germinating soybean seeds (Glycine max L. Mer. Cultivar Amsoy) and seedlings were studied by using light and transmission electron microscopy. When germinating began, the cotyledon tissues were packed with protein an lipid bodies. Mobilization of the reserves started in epidermis and vascular bundles. After three days of seedling growth, significant reductions of protein and lipid bodies were observed; concurrently, the numbers of starch grains, glyoxysoms, and mitochondria were increased. These ultrastructural changes are discussed with reference to the metabolism of the germinating soybean seeds and seedlings.

• Applied Microscopy
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• 제25권1호
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• pp.15-29
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• 1995

Legumin was purified from the endosperm cells of the ginseng seed and analyzed its characteristics. Distributional patterns of the legumin in the endosperm cells were identified using the immunocytochemical method. Legumin was glycoprotein composed of two subunits, molecular weights about 33,000 and 25,000 respectively. The molecular shape of purified legumin stained negatively seems to have hexagonal structure about 10 nm in size. It was localized at the rER, dictyosomes, and in the vacuoles at the early developing stage. Legumin was glycosylated in the dictyosomes and transported from the dictyosomes to the vacuoles. Legumin was accumulated into the central vacuole via the dictyosomes while the endosperm cells were developing. The armorphous proteins containing legumin were scattered randomly within the central vacuoles, which were aggregated together and became gradually spherical shape. Legumin was distributed within the globular protein bodies in the endosperm cells of matured seed. However legumin was not found in the globoids located in the protein bodies.

• 한국양식학회:학술대회논문집
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• 한국양식학회 2006년도 수산관련학회 공동학술대회 발표요지집
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• pp.522-523
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• 2006

• 한국식물병리학회지
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• 제10권4호
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• pp.261-269
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• 1994

One hundred and ninety two isolates of Armillaria were obtained from mycelial fans on infected hosts, rhizomorphs, and single basidiospores or trauma tissue of fruiting bodies. Mating tests showed that two of these isolates were A. mellea, eight were A. tabescens, 20 were A. ostoyae, and 162 were A. gallica. Armillaria ostoyae was mainly isolated from Pinus koraiensis and Qurecus spp., A. tabescens from fruiting bodies on Pinus densiflora and Qurecus spp., and A. gallica from many tree species but not Pinus koraiensis. Armillaria mellea, A. gallica, A. ostoyae and A. tabescens showed distinct protein banding patterns. Mycelial growth and rhizomorph formation was good on basal medium with ethanol added. A. gallica and A. mellea formed many rhizomorphs, but A. ostoyae did not. A. gallica showed the best rhizomorph formation on media with tannic acid and ethanol, but a. mellea formed the most rhizomorphs on gallic acid. Rhizomorphs showed monopodial branching for A. gallica and dichotomous branching for A. ostoyae. Fruiting bodies. formed in the laboratory on sawdust media most abundantly by A. tabescens. In nature, fruit body formation by A. tabescens was from early to mid August. A. ostoyae and A. gallica fruit bodies were formed from early August to late October. While there are common names in Korea for A. mellea and A. tabescens, such as mulberry mushroom relative, no common names are available for A. gallica and A. ostoyae. Therefore, we refer to a. gallica as the Gastrodia mushroom because it has been used to produce Gastrodia and A. ostoyae as the Korean pine mushroom because it is frequently found as mushrooms on Korean pine.

• 한국식품과학회지
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• 제20권1호
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• pp.72-78
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• 1988

열대지방에서 재배되는 18종의 콩종자의 구조적인 특성을 분류하기 위하여 그 미세구조를 주로 광학현미경으로 조사하였다. vicieae에 속하는 종실들은 많은 단일전분입자들로 구성된 자엽세포구조를 갖는 starch-rich legume이였으며, phaseoleae중에서는 benas(phaseolus), cow pea, green gram(vigna), hyacinth bean(dolicholus)이 starch-rich legume이였다. 한편 soybean(glycine), winged bean(psophocarpus)는 자엽세포가 대부분 protein body로 구성된 protein-rich legume이고 yam bean (pachyrrhizus)와 cluster bean(cyamopsis)에서는 protein body 보이는 구형물질로 이루어진 자엽세포 구조를 볼 수 있었다. 또한 green gram과 winged bean은 soybean에 비하여 두꺼운 세포벽을 갖고 있었으며 pit-pair가 관찰되었다. Lipid body는 winged bean과 soybean에서 볼 수 있었다. starch-rich legume들은 팥고물 제조과정에서 전분입자들이 파괴되지 않음으로써 특징적인 조직감을 부여하는 red bean이나 benas와 같은 phaseolus의 대체 자원으로 제시될 수 있었다.

• Journal of Microbiology and Biotechnology
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• 제10권5호
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• pp.632-637
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• 2000

This research was undertaken to restore the biological activity of cyclodextrin glucanotransferase (CGTase) of Bacillus macerans origin expressed as inclusion bodies in recombinant Escherichia coli. The optimum concentration of urea used as a denaturant was 8 M. The supplementation of 0.5 M urea into a dialysis buffer increased the refolding efficiency by preventing any protein aggregation. The influence of the protein concentration, temperature, and pH were also investigated. The protein concentration was found to be the most important factor in the refolding efficiency. The optimum temperature was 15-$25^{\circ}C$ and the optimum pH was 6.0. The maximum specific activity of the CGTase refolded under the optimum conditions was 92.2 U/mg, corresponding to 72% of the native CGTase. A comparison of the secondary structure between the native and the refolded CGTase showed that the relative ratio of the $\alpha$-helix content in the native to the refolded CGTase was 1:0.82.

• Journal of Plant Biology
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• 제35권2호
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• pp.99-106
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• 1992

인삼(Panax ginseng C.A. Meyer) 종자단백질인 vicilin을 ammonium sulfate 침전, gel permeation 및 이온 교환 크로마토그래피로 정제하였다. Vicilin은 분자량 55,000(큰 소단위) 및 44,000(작은 소단위)인 두 종의 소단위를 포함하는 당단백질이다. Vicilin에 대한 항체를 토끼에서 형성시켜 DEAE-Affi-Gel Blue affinity 크로마토그래피로 정제하였다. 이 항체와 금 입자가 결합된 2차 항체를 종자의 배유세포에 반응시켰다. 금 입자는 배유세포내의 단백질체, 전자밀도가 높은 과립 및 골지체의 elaborating 과립에 표지되었다. 이러한 결과는 조면소포체에서 합성되어 골지체로 수송된 vicilin이 골지의 소포내에서 공정과정을 거쳐 전자밀도가 높은 과립이 된 다음 단백질로 수송됨을 나타낸다.

• 한국작물학회:학술대회논문집
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• 한국작물학회 2017년도 9th Asian Crop Science Association conference
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• pp.115-115
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• 2017

Zinc finger proteins constitute a large family which has been studied to have various functions in different organisms. Tandem CCCH zinc finger proteins (TZFs), members of the zinc finger protein family, are known to participate as post-transcriptional regulators of gene expression in eukaryotes. Here, we showed that the OsZn15, a gene for tandem CCCH zinc finger protein, is induced by abiotic stress and its overexpression in transgenic rice plants (PGD1:OsZn15) gains higher drought tolerance. Gene expression analysis of promoter:GFP plants revealed that OsZn15 is specifically expressed in anther and embryo, but not in vegetative organs. In-field evaluation, grain yield was higher in the PGD1:OsZn15 than nontransgenic plants under drought conditions. Interestingly, OsZn15 is shown to not only localize at nucleus but also co-localize with both processing bodies (PB) and stress granules (SG), two messenger ribo-nucleoprotein complexes which are known to activate by forming cytoplasmic foci under stress conditions. In sum, these results suggest that OsZn15 increases drought stress tolerance of rice probably by participating in RNA turnover in PB and SG.

• Applied Biological Chemistry
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• 제32권1호
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• pp.64-72
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• 1989

Near full length cDNA clones encoding the rice seed storage protein, prolamine, were isolated and divided into two homology classes based on cross-hybridization and DNA sequencing analysis. These cDNA clones contain a single open reading frame encoding a putative rice prolamine precursor(M.W.=17,200) possessing atypical 14 amino acid signal peptide. Clones of these two homology classes diverge mainly by insertions/deletions of short nucleotide stretches and point mutations. The deduced primary structures of both types of prolamine polypeptides are devoid of any major tandem repetitive sequences, a feature prevalent in other cereal prolamines. No significant homology teas detected between the rice prolamine and other cereal prolamines, indicating that the rice gene evolved from a different ancestor that gave rise to other cereal prolamine genes. Developing wheat and rice endosperms were examined using ultrathin sections prepared from tissues harvested at various days after flowering. By immunocytochemical localization techniques, wheat prolamines are localized within vesicles from Golgi apparatus and in homogeneous regions of protein bodies. The involvement of the goli apparatus in the packaging of wheat prolamines into protein bodies indicates a pathway which differs from the mode of other cereal prolamines and resembles the mechanism employed for the storage of rice glutelin and legume globulins.