Linked Life Data

25181

Source:http://linkedlifedata.com/resource/pubmed/id/25181

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1978-6-12
pubmed:abstractText
Crude cell wall preparations from Cicer arietinum L. cell suspension cultures show high activity for the hydrolysis of coniferyl alcohol beta-D-glucoside (coniferin). Various beta-glucosidase activities could be solubilized from these preparations by 0.5 M NaCl treatment and one of these could be shown to possess a high activity for the hydrolysis of coniferin. The enzyme activities were purified to near homogeneity by Sephadex G-200 and CM-Sephadex chromatography. Isoelectric focussing indicated the occurrence of beta-glucosidase isoenzymes with identical catalytic activity (pI 8.5-10). Molecular weights were determined as 110 000, with two subunits of 63 000 and 43 000. Maximum hydrolytic activity is at pH 5. The beta-glucosidase isoenzymes catalyze the hydrolysis of various beta-glucosides with aromatic aglycone structure and different sugar moieties. However, coniferin has been found to be one of the best substrates (km = 0.8 mM; V = 6 mumol.min-1.mg protein-1) for these beta-glucosidase isoenzymes. The data suggest that beta-glucosidase-catalyzed reaction might be involved in lignification of these plant cell cultures.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
84
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
487-92
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
Characterization of beta-glucosidase isoenzymes possibly involved in lignification from chick pea (Cicer arietinum L.) cell suspension cultures.
pubmed:publicationType
Journal Article