Linked Life Data

6771250

Source:http://linkedlifedata.com/resource/pubmed/id/6771250

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1980-9-23
pubmed:abstractText
Kinetic studies of the two beta-glucosidase isozymes, GB-1 and GB-2, which were from the culture filtrate of a phytopathogenic fungus Pyricularia oryzae, revaled that the latter isozyme was an allosteric protein with two substrate binding sites. The homotropic effects of o- and m-nitrophenyl-beta-D-glucosides on GB-2 showed positive cooperativity, whereas that of cell cellooligosaccharide showed negative cooperatively. The affinity of GB-2 for cellooligosaccharide tended to increase with decreasing chain length, in contrast to that of GB-1. Glucono-delta-lactone and glucose acted as competitive inhibitors of GB-1 and GB-2. As regards the control of the level of glucose formed by the cellulose system, it appears that the rate of formation of glucose by beta-glucosidase is reduced by the presence of the substrate, cellooligosaccharide, as well as by the product, glucose.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
87
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1203-8
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Studies on cellulases of a phytopathogenic fungus, Pyricularia oryzae Cavara. IV. Kinetic studies on beta-glucosidases.
pubmed:publicationType
Journal Article