Linked Life Data

2962967

Source:http://linkedlifedata.com/resource/pubmed/id/2962967

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1988-3-2
pubmed:abstractText
Phosphoglucomutase can bind both negative and positive ions so that it may change its net electric charge according to the buffer species of the medium. For this reason the knowledge of the pIs of the erythrocyte phosphoglucomutase isoenzymes is not sufficient to forecast their separability by procedures based on charge separations such as ion exchange chromatography. In this paper we indicate the condition to obtain a satisfactory separation of the main erythrocyte phosphoglucomutase isoenzymes by DEAE-cellulose column chromatography. The pI values of the isolated isoenzymes are also reported and compared to those measured by others on whole hemolysates.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0021-2938
pubmed:author
pubmed:issnType
Print
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
267-74
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Isoelectric points and charge-dependent separation of erythrocyte phosphoglucomutase isoenzymes (PGM1 and PGM2).
pubmed:affiliation
Instituto di Chimica Biologica, Università di Urbino.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't