Linked Life Data

3718675

Source:http://linkedlifedata.com/resource/pubmed/id/3718675

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1986-7-31
pubmed:abstractText
A method is described for the purification of the alpha-mannosidase from Canavalia ensiformis. By three consecutive steps, a more than 500-fold purification is achieved and the pure enzyme obtained in 75% yield. One of these steps utilizes the specific interaction of the alpha-mannosidase with concanavalin A, the lectin from the same plant. This interaction is dependent on pH and ionic strength but does not involve the sugar binding site of the lectin. The interaction between both proteins may be important also in vivo.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0177-3593
pubmed:author
pubmed:issnType
Print
pubmed:volume
367
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
313-20
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Isolation of the Canavalia ensiformis seed alpha-mannosidase by chromatography on concanavalin A, the lectin from the same plant, without involving its sugar binding site.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't