Linked Life Data

40530

Source:http://linkedlifedata.com/resource/pubmed/id/40530

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1979-12-27
pubmed:abstractText
Mycelial and yeast forms of P. brasiliensis were tested for several glucohydrolases. In addition to high levels of beta-glucanases, low amounts of alpha-glucanase, chitinase and maltase were found. Tests for invertase, amylase and lactase were negative. The levels of beta-1,3-glucanase were higher in the mycelial form. The shift to the mycelial phase correlated with an increase in the levels of beta-1,3-glucanase. The enzyme was present in the cytoplasm, cell wall and culture medium. The extracellular enzyme was purified 42 fold by ammonium sulphate precipitation and gel filtration. Maximal activity was obtained at 60 degrees C and pH of 5.0 (acetate buffer or pH 6.0 (phosphate buffer). Its Km was 0.205 mg/ml. The cell wall-bound enzyme showed a higher temperature optimum. Optimum pH and Km were also slightly different. Following treatment of the cell walls with chitinase, beta-1,3-glucanase was released into the medium.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0003-6072
pubmed:author
pubmed:issnType
Print
pubmed:volume
45
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
265-74
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Beta-1-3-glucanase and dimorphism in Paracoccidioides brasiliensis.
pubmed:publicationType
Journal Article