| pubmed-article:12884086 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12884086 | lifeskim:mentions | umls-concept:C0003308 | lld:lifeskim |
| pubmed-article:12884086 | lifeskim:mentions | umls-concept:C1524059 | lld:lifeskim |
| pubmed-article:12884086 | lifeskim:mentions | umls-concept:C0008145 | lld:lifeskim |
| pubmed-article:12884086 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:12884086 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:12884086 | pubmed:dateCreated | 2003-10-2 | lld:pubmed |
| pubmed-article:12884086 | pubmed:abstractText | The mode of action of two chitinases from the Antarctic Arthrobacter sp. strain TAD20 on N-acetyl-chitooligomers and chitin polymers has been elucidated. Identification of the length of chitin oligomers following enzymatic hydrolysis was verified by using HPLC-based analysis. It was observed that the length of the oligomer is important for enzyme action. The enzymes cannot effectively hydrolyze chitin oligomers with a degree of polymerization lower than four. ArChiA is an endochitinase which hydrolyzes chitin substrates randomly, whereas ArChiB is an exochitinase which degrades chitin chains and N-acetyl-chitooligomers from the nonreducing end, releasing N- N'-diacetyl-chitobiose. ArChiB (100 microg/ml) inhibited spore germination and hyphal elongation of the phytopathogenic fungus Botrytis cinerea by 15% and 30%, respectively. A more pronounced effect was observed with ArChiA (100 microg/ml) resulting in 70% inhibition of spore germination and 60% inhibition of germ tube elongation. A slight additive effect was observed, when the two enzymes were used in combination, only on the inhibition of germ tube elongation. | lld:pubmed |
| pubmed-article:12884086 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12884086 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12884086 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12884086 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12884086 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12884086 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12884086 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12884086 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12884086 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:12884086 | pubmed:issn | 1431-0651 | lld:pubmed |
| pubmed-article:12884086 | pubmed:author | pubmed-author:BouriotisVass... | lld:pubmed |
| pubmed-article:12884086 | pubmed:author | pubmed-author:MavromatisKon... | lld:pubmed |
| pubmed-article:12884086 | pubmed:author | pubmed-author:LoritoMatteoM | lld:pubmed |
| pubmed-article:12884086 | pubmed:author | pubmed-author:WooSheridan... | lld:pubmed |
| pubmed-article:12884086 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12884086 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:12884086 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12884086 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12884086 | pubmed:pagination | 385-90 | lld:pubmed |
| pubmed-article:12884086 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:12884086 | pubmed:meshHeading | pubmed-meshheading:12884086... | lld:pubmed |
| pubmed-article:12884086 | pubmed:meshHeading | pubmed-meshheading:12884086... | lld:pubmed |
| pubmed-article:12884086 | pubmed:meshHeading | pubmed-meshheading:12884086... | lld:pubmed |
| pubmed-article:12884086 | pubmed:meshHeading | pubmed-meshheading:12884086... | lld:pubmed |
| pubmed-article:12884086 | pubmed:meshHeading | pubmed-meshheading:12884086... | lld:pubmed |
| pubmed-article:12884086 | pubmed:meshHeading | pubmed-meshheading:12884086... | lld:pubmed |
| pubmed-article:12884086 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12884086 | pubmed:articleTitle | Mode of action and antifungal properties of two cold-adapted chitinases. | lld:pubmed |
| pubmed-article:12884086 | pubmed:affiliation | Department of Biology, Division of Applied Biology and Biotechnology, University of Crete, PO Box 1470, 71110 Heraklion, Crete, Greece. | lld:pubmed |
| pubmed-article:12884086 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12884086 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
