Linked Life Data

9892065

Source:http://linkedlifedata.com/resource/pubmed/id/9892065

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1999-3-23
pubmed:abstractText
Human GH isoforms were separated by anion-exchange chromatography using a linear NaCl gradient in the presence and absence of EDTA and EGTA. SDS-PAGE showed that glycosylated 24-kDa hGH did not appreciably separate from other hGH variants in the absence of metal chelators. However, in the presence of metal chelators, glycosylated 24-kDa hGH separated from the bulk of the hGH isoforms. Human GH isoforms were also separated by size-exclusion chromatography in the presence and absence of metal chelators. Glycosylated 24-kDa hGH eluted with the bulk of the hGH isoforms in both separations. The inclusion of metal chelators in chromatographic buffers to alter the charge and/or size of proteins by stripping their metals may be a generally useful strategy in their fractionation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1387-2273
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
720
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
39-47
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Divalent metal cation chelators enhance chromatographic separation of structurally similar macromolecules: separation of human growth hormone isoforms.
pubmed:affiliation
Division of Life Sciences, The University of Texas at San Antonio, 78249-0609, USA. lharo@lonestar.utsa.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.