지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2005.12
- 수록면
- 301 - 309 (9page)
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초록· 키워드
오류제보하기
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, α-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-l,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.
목차
Materials and Methods
Discussion
References
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UCI(KEPA) : I410-ECN-0101-2009-481-017570792