Linked Life Data

7190436

Source:http://linkedlifedata.com/resource/pubmed/id/7190436

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1980-10-21
pubmed:abstractText
Androgen binding protein (ABP) was purified from rat epididymides by sequential ammonium sulfate precipitation, affinity chromatography, gel filtration, and DEAE ion exchange chromatography. The column matrix formed by coupling dihydrotestosterone-17 alpha-(hexanoic acidY to agarose via diisopropylamine was stable during the extensive washing required following application of crude tissue extracts to the affinity matrix. In addition, when used under the optimal conditions, the column produced a 1600-fold purified in a single step. Apparent homogeneity of the final product was shown by polyacrylamide gel electrophoresis, sedimentation equilibrium, and constant specific activity across the peak of the final chromatograph. The molecular weight determined by sedimentation equilibrium at pH 7.4 was 85 000. By contrast, the molecular weight determined by sedimentation equilibrium in guanidine.HCl and by sodium dodecyl sulfate-polyacrylamide gel electrophoresis was approximately one-half that of the native protein, suggesting that suggesting that ABP is comprised of subunits.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2853-60
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Purification and characterization of androgen binding protein from the rat epididymis.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.