Linked Life Data

7398623

Source:http://linkedlifedata.com/resource/pubmed/id/7398623

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1980-10-24
pubmed:abstractText
The properties of three types of adsorbents obtained by coupling oestradiol 7 alpha-derivatives to agarose were compared. The adsorbents examined were: oestradiol 7 alpha-decamethylene-agarose, oestradiol 7 alpha-decamethylene-poly(anayl-lysine)-agarose and oestradiol 7 alpha-trimethylene-poly(alanyl-lysine)-agarose. The following results were obtained. (1) All these adsorbents are stable at 0 degrees C for a least a year when stored in water. In the presence of cytosol they are stable for several hours and are reusable after a simple wash. (2) A new method allowing the calculation of the maximala receptor binding capacity of an absorbent was developed. (3) The geometry of the column and the dynamics of the loading have no influence on the binding capacity of the adsorbents. (4) Binding of the cytosol receptor to the adsorbent depends on whether the receptor had previously been partially purified by heparin-Ultrogel chromatography or treated with low or high salt concentration or trypsin. It was demonstrated that aggregation decreases the binding of the receptor to the adsorbents. (5) A satisfactory recovery of receptor upon elution is possible only with biospecific adsorbents containing low concentrations of coupled steroid (less than or equal to 0.2 mg/ml). The use of these adsorbents for the purification of the trypsin-treated receptor directly from cytosol allowed a 2500-fold purification corresponding to 5% pure protein (assuming one oestradiol binding site per molecule of Mr 60000). When starting from a low salt preparation containing the native 8-S receptor, partially purified by heparin-Ultrogel chromatography, preliminary experiments using affinity chromatography gave a further purification of 250--500-fold and led to a 50--90% pure protein (assuming one oestradiol binding site per molecule of Mr 70000).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
106
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
481-93
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Properties of biospecific adsorbents, obtained by immobilization of oestradiol 7 alpha-derivatives, for purification of calf-uterine cytosol oestradiol receptor.
pubmed:publicationType
Journal Article, Comparative Study