Linked Life Data

1369314

Source:http://linkedlifedata.com/resource/pubmed/id/1369314

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1991-7-11
pubmed:abstractText
This paper describes the specificity of Aspergillus niger 5-16 alpha-galactosidase toward various oligosaccharides having terminal galactose or stub galactose or both on the oligosaccharide. The galactosidase rapidly hydrolyzed p-nitrophenyl-alpha-D-galactopyranoside, but hardly liberated galactose from melibiose, manninotriose, 6(3)-alpha-D-galactosylmannotriose, etc. On the other hand, the enzyme tore off the stub galactoses attached to the inner mannoses of the main-chain of galactomannooligosaccharides, but not the terminal galactoses attached to the non-reducing-end mannoses of the main-chain. Thus, the substrate specificity of A. niger 5-16 alpha-galactosidase is quite different from that of Mortierella vinacea alpha-galactosidase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
B
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0002-1369
pubmed:author
pubmed:issnType
Print
pubmed:volume
55
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
109-15
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Substrate specificity of alpha-galactosidase from Aspergillus niger 5-16.
pubmed:affiliation
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
pubmed:publicationType
Journal Article, Comparative Study