Linked Life Data

6841273

Source:http://linkedlifedata.com/resource/pubmed/id/6841273

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1983-6-10
pubmed:abstractText
High resolution, two-dimensional PAGE was used to characterize purified plasma membranes (PM) from boar spermatozoa. In addition to the abundance of polypeptides resolved, unusual features of PM discerned in gel patterns include a large number of basic polypeptides and the presence of at least three polypeptides with molecular weights in excess of 200 K daltons. In order to reduce these large numbers of polypeptides into smaller fractions, an important step in developing a surface map of these membranes, detergent-solubilized membranes were fractionated by the techniques of ion exchange chromatography and lectin affinity chromatography. PM polypeptides, solubilized in the nonionic detergents, were fractionated on DEAE Sephadex using phosphate ion gradients containing EDTA. Most of the major acidic polypeptides were eluted as a group at high phosphate ion concentrations. Membrane polypeptides can be separated into smaller populations by affinity chromatography on wheat germ agglutinin-agarose (WGA) or by Concanavalin A-agarose. Concanavalin A-agarose binds most PM glycoproteins, but partial purification of an important group of very basic proteins was obtained by repeated chromatography of polypeptides that failed to bind to this lectin. Since biologic activity (including immunologic potency) is often retained in the detergents used, the ability to fractionate the major polypeptide of the boar sperm PM into different and much smaller populations in large quantity and to characterize these proteins by electrophoresis provides a starting point for determining the functional significance and location of the major surface proteins of the boar sperm PM.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0196-3635
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
71-81
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:articleTitle
Characterization of boar sperm plasma membranes by two-dimensional PAGE and isolation of specific groups of polypeptides by anion exchange chromatography and lectin affinity chromatography.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.