Confirmation of non N-glycan linked mannose glycosylation in chitinase 42 kDa secreted by Trichoderma harzianum BIO10671
Citinase 42 kDa produced by Trichoderma harzianum has been proven as a prime compund to be excreted onto the hyphae of the pathogen causing localised cell wall lysis at the point of interaction. This finally initiate the process of the host cell becomes empty of cytoplasm, disintegrates and shows a...
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| Format: | Article |
| Language: | English |
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Academic Journals
2008
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| Online Access: | http://psasir.upm.edu.my/id/eprint/4698/ http://psasir.upm.edu.my/id/eprint/4698/1/13.pdf |
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| author | Mustafa, Muskhazli Qamaruz Zaman, Faridah Ramli, Salfarina Tohfah, Nor Farizan Ithnin, Nalisha Wallis, Gregg L. F. |
| author_facet | Mustafa, Muskhazli Qamaruz Zaman, Faridah Ramli, Salfarina Tohfah, Nor Farizan Ithnin, Nalisha Wallis, Gregg L. F. |
| author_sort | Mustafa, Muskhazli |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | Citinase 42 kDa produced by Trichoderma harzianum has been proven as a prime compund to be excreted onto the hyphae of the pathogen causing localised cell wall lysis at the point of interaction. This finally initiate the process of the host cell becomes empty of cytoplasm, disintegrates and shows a rapid collapse. This study investigates the existence of N-glyan linked mannose in chitinase 42 kDa from T.harzianum BIO10671 was initially purified using anion exchange chromatography prior to a series of experiments such as immunoblotting against the chitinase 42 kDa antibody, lectin staining for detecting any terminal linked mannose and galactofuranose detection to determine the presence of galactofuranose components in glycoproteins. The enzyme purification varvested about 12-fold of chitinase 42 kDa after overnight incubation in chitinase 42 kDa antibody suggesting taht the gene for chitinase 42 kDa was greatly expressed in this strain.There are no intervation of galactofuranose on any of the terminal mannose in chitinase 42 kDa as shown by negative results on samples treated with or without endoglycosidase-H and lectin staining. Therefore, it can be concluded that glycosylation occured in the chitinase 42 kDa from T.harianum 42 kDa was not in the form of N-glycan linked mannose as aspected. |
| first_indexed | 2025-11-15T07:18:41Z |
| format | Article |
| id | upm-4698 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T07:18:41Z |
| publishDate | 2008 |
| publisher | Academic Journals |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-46982017-10-27T03:50:47Z http://psasir.upm.edu.my/id/eprint/4698/ Confirmation of non N-glycan linked mannose glycosylation in chitinase 42 kDa secreted by Trichoderma harzianum BIO10671 Mustafa, Muskhazli Qamaruz Zaman, Faridah Ramli, Salfarina Tohfah, Nor Farizan Ithnin, Nalisha Wallis, Gregg L. F. Citinase 42 kDa produced by Trichoderma harzianum has been proven as a prime compund to be excreted onto the hyphae of the pathogen causing localised cell wall lysis at the point of interaction. This finally initiate the process of the host cell becomes empty of cytoplasm, disintegrates and shows a rapid collapse. This study investigates the existence of N-glyan linked mannose in chitinase 42 kDa from T.harzianum BIO10671 was initially purified using anion exchange chromatography prior to a series of experiments such as immunoblotting against the chitinase 42 kDa antibody, lectin staining for detecting any terminal linked mannose and galactofuranose detection to determine the presence of galactofuranose components in glycoproteins. The enzyme purification varvested about 12-fold of chitinase 42 kDa after overnight incubation in chitinase 42 kDa antibody suggesting taht the gene for chitinase 42 kDa was greatly expressed in this strain.There are no intervation of galactofuranose on any of the terminal mannose in chitinase 42 kDa as shown by negative results on samples treated with or without endoglycosidase-H and lectin staining. Therefore, it can be concluded that glycosylation occured in the chitinase 42 kDa from T.harianum 42 kDa was not in the form of N-glycan linked mannose as aspected. Academic Journals 2008 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/4698/1/13.pdf Mustafa, Muskhazli and Qamaruz Zaman, Faridah and Ramli, Salfarina and Tohfah, Nor Farizan and Ithnin, Nalisha and Wallis, Gregg L. F. (2008) Confirmation of non N-glycan linked mannose glycosylation in chitinase 42 kDa secreted by Trichoderma harzianum BIO10671. Asian Journal of Biochemistry, 3 (4). pp. 235-242. ISSN 1815-9923; ESSN: 1815-9931 http://www.scialert.net/abstract/?doi=ajb.2008.235.242 10.3923/ajb.2008.235.242 |
| spellingShingle | Mustafa, Muskhazli Qamaruz Zaman, Faridah Ramli, Salfarina Tohfah, Nor Farizan Ithnin, Nalisha Wallis, Gregg L. F. Confirmation of non N-glycan linked mannose glycosylation in chitinase 42 kDa secreted by Trichoderma harzianum BIO10671 |
| title | Confirmation of non N-glycan linked mannose glycosylation in chitinase 42 kDa secreted by Trichoderma harzianum BIO10671 |
| title_full | Confirmation of non N-glycan linked mannose glycosylation in chitinase 42 kDa secreted by Trichoderma harzianum BIO10671 |
| title_fullStr | Confirmation of non N-glycan linked mannose glycosylation in chitinase 42 kDa secreted by Trichoderma harzianum BIO10671 |
| title_full_unstemmed | Confirmation of non N-glycan linked mannose glycosylation in chitinase 42 kDa secreted by Trichoderma harzianum BIO10671 |
| title_short | Confirmation of non N-glycan linked mannose glycosylation in chitinase 42 kDa secreted by Trichoderma harzianum BIO10671 |
| title_sort | confirmation of non n-glycan linked mannose glycosylation in chitinase 42 kda secreted by trichoderma harzianum bio10671 |
| url | http://psasir.upm.edu.my/id/eprint/4698/ http://psasir.upm.edu.my/id/eprint/4698/ http://psasir.upm.edu.my/id/eprint/4698/ http://psasir.upm.edu.my/id/eprint/4698/1/13.pdf |