Linked Life Data

8938373

Source:http://linkedlifedata.com/resource/pubmed/id/8938373

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-1-2
pubmed:abstractText
Identification of key enzymes of sapstain fungi which cause wood discoloration is necessary for targeted inhibition strategies. Therefore proteinases involved in the nitrogen pathway have been characterized. The sap-staining fungus Ophiostoma piceae strain 387N produced proteolytic enzymes when grown on wood and protein-supplemented media. Proteolytic activity in culture filtrates was inhibited by PMSF and EDTA. The major protein in culture filtrates was a proteinase with a pI of 5.6 and a molecular weight of 33 kDa. This was the major proteinase produced by O. piceae and it was purified from culture filtrates by hydrophobic interaction chromatography. The proteinase was susceptible to autolytic degradation during chromatographic separations when ammonium sulfate was not present. When azocoll was used as a substrate, the proteolytic activity of the purified proteinase was determined to be optimal at pH 7-9 and 40 degrees C. Similar pH and temperature optima were obtained using succinyl-ala-ala-pro-phe-p-nitroanilide as the substrate. The N-terminal sequence of the protein showed a high degree of homology with fungal alkaline serine proteinases classified as subtilisin class II enzymes. Agreement in inhibition patterns and electrophoretic and catalytic properties suggested the secretion of the same proteinase during growth on wood. Understanding the role of this proteinase during fungal colonization is an important step toward disrupting fungal growth on wood.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
B
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0141-0229
pubmed:author
pubmed:issnType
Print
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
133-40
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Isolation and characterization of a subtilisin-like serine proteinase secreted by the sap-staining fungus Ophiostoma piceae.
pubmed:affiliation
Department of Wood Science, Faculty of Forestry, University of British Columbia, Vancouver, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't