DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, KO | ko |
dc.contributor.author | Kim, MG | ko |
dc.contributor.author | Jang, HH | ko |
dc.contributor.author | Lee, JY | ko |
dc.contributor.author | Kim, Sun-Chang | ko |
dc.contributor.author | Lee, SY | ko |
dc.date.accessioned | 2013-03-02T18:17:45Z | - |
dc.date.available | 2013-03-02T18:17:45Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 1999-11 | - |
dc.identifier.citation | JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, v.32, no.6, pp.541 - 546 | - |
dc.identifier.issn | 1225-8687 | - |
dc.identifier.uri | http://hdl.handle.net/10203/74859 | - |
dc.description.abstract | When we compared the chitinase activity of various plant sources using colorimetric or active gel-staining assay methods, the specific activity of pumpkin leaves was the highest among the samples we analyzed. The highly active chitinase from pumpkin leaves (designated PL-ChtIII) was purified to homogeneity using affinity chitin gel and HPLC Mono-Q anion-exchange column chromatographies, In contrast to other members of the class III chitinase family, PL-ChtIII showed a strong binding affinity to the regenerated chitin gel column. The apparent molecular weight of PL-ChtIII was estimated to be 29 kDa on SDS-PAGE gel, while its optimum pH and temperature were shown to be pH 6.0 and 60 degrees C, respectively. Analyzing the reaction products of PL-ChtIII with swollen chitin as substrate, the dimer and tetramer of N-acetylglucosamine were produced as major products in the first hour of the enzymatic reaction along with a small amount of monomers and trimers, As the reaction time increased, dimeric N-acetylglucosamine became the predominant form of reaction product. | - |
dc.language | English | - |
dc.publisher | SPRINGER-VERLAG SINGAPORE PTE LTD | - |
dc.subject | PATHOGENESIS-RELATED PROTEINS | - |
dc.subject | BEAN-LEAVES | - |
dc.subject | WHEAT-GERM | - |
dc.subject | ETHYLENE | - |
dc.subject | ENDOCHITINASE | - |
dc.subject | PURIFICATION | - |
dc.subject | TOBACCO | - |
dc.subject | CLONING | - |
dc.subject | GENES | - |
dc.title | Biochemical properties of a chitin-binding class III chitinase in pumpkin leaves | - |
dc.type | Article | - |
dc.identifier.wosid | 000083911400004 | - |
dc.identifier.scopusid | 2-s2.0-0348203022 | - |
dc.type.rims | ART | - |
dc.citation.volume | 32 | - |
dc.citation.issue | 6 | - |
dc.citation.beginningpage | 541 | - |
dc.citation.endingpage | 546 | - |
dc.citation.publicationname | JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY | - |
dc.contributor.localauthor | Kim, Sun-Chang | - |
dc.contributor.nonIdAuthor | Lee, KO | - |
dc.contributor.nonIdAuthor | Kim, MG | - |
dc.contributor.nonIdAuthor | Jang, HH | - |
dc.contributor.nonIdAuthor | Lee, JY | - |
dc.contributor.nonIdAuthor | Lee, SY | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | chitin binding activity | - |
dc.subject.keywordAuthor | class III chitinase | - |
dc.subject.keywordAuthor | enzymatic properties | - |
dc.subject.keywordAuthor | pumpkin leaves | - |
dc.subject.keywordPlus | PATHOGENESIS-RELATED PROTEINS | - |
dc.subject.keywordPlus | BEAN-LEAVES | - |
dc.subject.keywordPlus | WHEAT-GERM | - |
dc.subject.keywordPlus | ETHYLENE | - |
dc.subject.keywordPlus | ENDOCHITINASE | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | TOBACCO | - |
dc.subject.keywordPlus | CLONING | - |
dc.subject.keywordPlus | GENES | - |
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