Linked Life Data

2045457

Source:http://linkedlifedata.com/resource/pubmed/id/2045457

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1991-7-18
pubmed:abstractText
Proteins, regardless of their origin, have to be highly purified, particularly from the immunochemical point of view, if they are to be used to study their allergenicity. It is shown that cat albumin, a highly potent allergen for cat-sensitive humans, can be isolated and purified from cat serum using immobilized metal ion affinity chromatography (copper ions) instead of a salting-out process or precipitation with alcohol, techniques generally used for the preparation of serum proteins. During the process described, immunoglobulins are concomitantly isolated in a relatively pure form. Cat albumin amino acid composition and sequence were analysed after an ultimate purification by ion-exchange chromatography. The highest homology (greater than 80%) was found with the rat serum albumin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9673
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
539
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
475-84
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Isolation and purification of cat albumin from cat serum by copper ion affinity chromatography: further analysis of its primary structure.
pubmed:affiliation
Unité d'Immuno-Allergie, Institut Pasteur, Paris, France.
pubmed:publicationType
Journal Article