Linked Life Data

10424454

Source:http://linkedlifedata.com/resource/pubmed/id/10424454

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1999-10-20
pubmed:abstractText
Migration across a stationary pH gradient results in the electrophoretic titration of a protein's dissociable groups. From the resulting curves, some properties of the protein may be derived, including overall amino acid composition and type of mutation between polymorphic variants, as well as range of stability or, for enzymes, of catalytic activity. Analysis with this technique is a stringent purity criterion; other applications allow the study of interacting systems and the planning of chromatographic fractionations based on differences in surface charge.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0173-0835
pubmed:author
pubmed:issnType
Print
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1325-38
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Low-tech electrophoresis, small but beautiful, and effective: electrophoretic titration curves of proteins.
pubmed:affiliation
Istituto di Scienze Farmacologiche, Facoltà di Farmacia, Università degli Studi di Milano, Italy. elisabetta.gianazza@unimi.it
pubmed:publicationType
Journal Article, Review