Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1979-10-24
pubmed:abstractText
Two methods of isolating Fab- and Fc-fragments from mouse immunoglobulin G1 are presented. The first method involves fractionation of papain protein hydrolysate on a column with DEAE- (or DE-32)-cellulose adjusted with 0.005 M K-phosphate buffer, pH 8. The Fab-fragment was eluted from the column with the starting buffer. The Fc-fragment was eluted, with the buffer ionic strength being increased to 0.4 M. Another method involves protein fractionation on an ion exchanger adjusted with 0.004 M Tris-H3PO4 buffer, pH 8.5. All the protein was column bound. The Fab-fragment was eluted with 0.04 M Tris-buffer containing a 0.004 M mixture of K-phosphates, pH 8.6. The Fc-fragment was eluted, with ionic strength being raised to 0.4 M with phosphates. As none of the methods assures isolation of absolutely pure Fab- or Fc-fragments, it is requird that cross absorption of antisera with respective immunosorbents may be carried on in order to obtain monospecific antisera to these fragments.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0365-9615
pubmed:author
pubmed:issnType
Print
pubmed:volume
88
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
116-9
pubmed:dateRevised
2008-10-8
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
[Isolation of FAB and Fc fragments from murine immunoglobulin G1].
pubmed:publicationType
Journal Article, English Abstract