Linked Life Data

3044336

Source:http://linkedlifedata.com/resource/pubmed/id/3044336

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
82
pubmed:dateCreated
1988-9-15
pubmed:abstractText
The presently known possibilities and conditions for achieving the crystallization of Albumin, Transthyretin, Retinol-binding Protein, Ceruloplasmin and beta 2-Glycoprotein I are described with respect to our own experiences. For isolating some proteins the crystallization gives rise to a real purification step. Sometimes degrees of purity near to 98 till 99% will be reached. Furthermore crystalline proteins are very important for the determination of the three-dimensional structure by aid of the X-ray diffraction analysis. For this purpose large single crystals are needed with minimum requirements of 0.4 mm length for all the three dimensions. Additionally the crystals must have a high degree of order on the molecular level and should allow recording of the diffraction pattern out to 3 A resolution. From the five proteins described here the three dimensional molecular structure of Transthyretin and Retinol-binding Protein could be elucidated by using the method of the X-ray diffraction analysis.
pubmed:language
ger
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0301-0457
pubmed:author
pubmed:issnType
Print
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
104-26
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
[Crystallized human plasma proteins. I. Albumin, transthyretin, retinol-binding protein, ceruloplasmin and beta 2-glycoprotein I].
pubmed:affiliation
Behringwerke Forschungslaboratorien, Marburg, Bundesrepublik Deutschland.
pubmed:publicationType
Journal Article, English Abstract, Review