Linked Life Data

8852722

Source:http://linkedlifedata.com/resource/pubmed/id/8852722

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-12-5
pubmed:abstractText
We have used free-solution capillary electrophoresis (FSCE) to separate three distinct mouse metallothionein (MT) isoforms, MT-1, MT-2 and MT-3. FSCE was conducted in an uncoated fused-silica capillary (57 cm x 50 microns I.D., 50 cm to detector) using 50 mM sodium phosphate buffer adjusted to pH 7.0 or 2.0. At neutral pH, each of the three isoform peaks were well resolved from a mixture with the order of migration (MT-1 > MT-2 > MT-3) related to the net negative charge on the protein. At acidic pH, the migration order was reversed with MT-3 migrating fastest, suggesting MT-3 had a higher net positive charge than MT-2 or MT-1. UV absorbance spectra (190-300 nm) confirmed the presence of Zn in MT-1 and MT-2. MT-3, which was saturated with Cd to stabilize the protein, gave a spectrum characteristic of the Cd-S charge transfer (shoulder at ca. 250 nm). At pH 2.0, the absorbance spectra for all three mouse MTs were characteristic of the metal-free form of the protein (apothionein). Thus, FSCE conducted at neutral pH separates MT isoforms with their metals intact, whereas at pH 2.0, both the Zn and the Cd dissociate from the protein during the run.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1572-6495
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
675
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
327-31
pubmed:dateRevised
2007-10-16
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Separation of three mouse metallothionein isoforms by free-solution capillary electrophoresis.
pubmed:affiliation
Agricultural Research Service, US Department of Agriculture, Beltsville, MD 20705-2350, USA.
pubmed:publicationType
Journal Article