• YAKHAK HOEJI
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• v.40 no.4
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• pp.387-393
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• 1996

The erythrocytes agglutination test was applied to the common korean plants for lectin activity screening by using human blood. During the four years, 108 species from 46 families of floras were collected, identified and subjected to the test after being divided into several different parts. Only 13 species demonstrated strong lectin activities. Meanwhile 66 species did not shown any agglutination. All others were observed as having low activity or as having hemolytic constituents.

• The Plant Pathology Journal
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• v.21 no.4
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• pp.301-309
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• 2005

Trichoderma species/isolates exhibited varied degree of agglutination on sclerotial (Sc) and hyphal (Hy) surface of Macrophomina phaseolina. The agglutination efficiencies on Sc and Hy ranged from $11\;to\;57\%$. Isolates of T. harzianum (Th) and T. viride (Tv) showed greater agglutination on Sc ($23-57\%$) and Hy ($16-47\%$). Different enzymes (trypsin, pepsin, proteinase k, a-chymotrypsin, lyticase and glucosidase) and inhibitors (tunicamycin, cycloheximide, brefeldin A, sodium azide, dithiothreitol and SDS) reduced the agglutination potential of conidia of Th-23/98 and Tv-25/98; however, the extent of response varied greatly in different treatments. Different fractions of Th-23/98 and Tv-25/98 exhibited haemagglutinating reaction with human blood group A, B, AB and O. Haemagglutinating activity was inhibited by different sugars and glycoproteins tested. Crude haemagglutinating protein from outer cell wall protein fraction of Th-23/98 and Tv-25/98 were eluted on Sephadex G-100 column. Initially Th-23/98 and Tv-25/98 exhibited two peaks showing no agglutination activity; however, lectin activity was detected in the third peak. Similar to crude lectin, the purified lectin also exhibited haemagglutinating activity with different erythrocyte source. SDS-PAGE analysis of partially purified lectin revealed single band with an estimated molecular mass of 55 and 52 kDa in Th-23/98 and Tv-25/98, respectively. Trypsin, chymotrypsin and b-1,3-glucanase totally inhibited lectin activity. Similarly, various pH also affected the haemagglutinating activity of Th-23/98 and Tv-25/98. From the present observations, it can be concluded that the recognition/attachment of mycoparasite (T. harzianum and T. viride) to the host surface (M. phaseolina) may be most likely due to lectin-carbohydrate interaction.

• Journal of Life Science
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• v.17 no.2 s.82
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• pp.254-259
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• 2007

Biochemical characterization of lectin isolated from fruit of cherry tomato through neutral saline extraction, ammonium sulfate precipitation, and affinity chromatography on Sephadex G-200 was studied. The lectin was agglutinated by trypsin-treated human ABO erythrocytes, and the most pronounced activity of agglutination was observed at B type erythrocyte. The analysis of the lectin by SDS-PAGE showed the high intensity band with molecular weights of 10.7 kDa. The optimal temperature and thermal stability of the lectin was $40^{\circ}C$ and $40-60^{\circ}C$, respectively. The maximal pH of this lectin was pH 7.2.

• KSBB Journal
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• v.23 no.1
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• pp.48-53
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• 2008

Lectin was isolated from locular fluid of tomato by affinity chromatography using Sephadex G-200, and studied its some biochemical properties. SDS-PAGE of the isolated lectin revealed a tetramer composed of two identical subunits with molecular weights of 39 and 23 kDa. The isolated lectin was agglutinated by trypsin-treated human ABO type blood erythrocytes with similar potency, and the most activity of agglutination was found at B type blood erythrocyte. This lectin showed maximum thermal stability at $70^{\circ}C$, and was relatively stable to heat with the higher activity at $40-80^{\circ}C$. The optimal temperature and pH of this lectin were $50^{\circ}C$ and pH 7.0, respectively.

• Korean journal of applied entomology
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• v.14 no.4 s.25
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• pp.193-198
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• 1975

This experiment was performed to clarify the concentration of rice stripe virus in the rice Plant leaves by serological test, and was attempted to inspect the virus carrier among small brown planthopper by antibody-sensitized hemagglutination test. The antiserum was prepared by injecting intervenously into the external marginal vein of the ear of a rabbit. The precipitin titer of it was 1 : 16. The rough virus fluid prepared from diseased leaves was centrifuged at 10.000 rpm, and then the supernatant solution was treated at $55^{\circ}C$ for 5 minutes and the solution clarified by removing the agglutinate was used as the antigen solution. Antibody-sensitized erythrocyte solution was prepared from sheep erythrocytes sensitized by rice stripe virus with tannic acid, and its agglutination titer was 1 : 512. The virus concentrations in flag leaves or first leaves just below them showing different symptoms was high with progressing the severity of symptoms. And the concentrations of the virus in leaves of varieties of the rice plant showing same degree symptom were lower in suscetible varieties, Sadominori, Palgoeng, Mangyong and Nihonbare, than in the resistant one, Tongil, but in Yooshin which was known as the resistant, lower rather than in Tongil. The reacton of antibody-sensitized hemagglutination test to inspect the virus carrier, was so highly sensitive that this reaction was recognized as a method which is able to Identify the carrier accurately in short time.