Linked Life Data

8323261

Source:http://linkedlifedata.com/resource/pubmed/id/8323261

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1993-8-5
pubmed:abstractText
beta-D-glucosidase purified from commercial preparations of clarified culture broth of Aspergillus niger (Novo SP188) was shown to elute as two distinct species during analytical anion-exchange chromatography (AEC). However, the two enzyme forms behaved identically on sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE), high-performance size-exclusion chromatography (HPSEC), and isoelectric focusing. Also, the N-terminal amino acid sequence, amino acid composition, fingerprint of tryptic-digest peptides, circular dichroism spectra, and reaction kinetics appear identical for these forms. This feature of the A. niger enzyme is distinctly different from beta-D-glucosidase isozymes reported from other sources, where multiple forms tend to differ in molecular weight and/or isoelectric pH. Michaelis-Menten kinetic analysis also gave comparable results for the two forms. The distinct behavior on AEC was explained by considering the differences in N-linked carbohydrates liberated from both species following treatment with endoglycosidase H or F.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0273-2289
pubmed:author
pubmed:issnType
Print
pubmed:volume
39-40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
213-25
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Isolation and characterization of two forms of beta-D-glucosidase from Aspergillus niger.
pubmed:affiliation
Applied Biological Sciences Branch, National Renewable Energy Laboratory, Golden, CO 80401.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.