Linked Life Data

2011130

Source:http://linkedlifedata.com/resource/pubmed/id/2011130

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1991-5-8
pubmed:abstractText
Four different proteases were screened for their capability of selectively digesting murine monoclonal IgGl to obtain active F(ab)2. For the screening, a series of five different mouse monoclonal antibodies (IgGl, k) was used, recognizing different tumor-associated antigens and currently used for radioimmunoimaging studies. The enzymes (pepsin, bromelain, ficin and elastase) showed different fragmentation capability and the fragments obtained showed different stability and immunoreactivity. No digestion was noticed using elastase. Pepsin gave discontinuous results, in that its activity ranged from reduction of IgG to small inactive fragments to an inability to digest the immunoglobulin. Pepsin activity was strongly pH-dependent and immunoreactivity of the obtained fragments was not always conserved. Bromelain and, in particular, ficin gave excellent results. Digestion was always rapid and stable, all five MAbs were reduced to F(ab)2 in a comparable time range and with high yields. Moreover, ficin-obtained F(ab)2 showed a highly conserved immunoreactivity. Therefore, ficin was selected as the murine monoclonal IgGl digestion enzyme to obtain active bivalent antibody fragments. The digestion procedure gave a uniform result for all five different MAbs and was easily scaled up to produce hundreds of milligrams of F(ab)2.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0161-5890
pubmed:author
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
69-77
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
A new enzymatic method to obtain high-yield F(ab)2 suitable for clinical use from mouse IgGl.
pubmed:affiliation
Biochemical Oncology Laboratory, SORIN Biomedica, Saluggia (VC), Italy.
pubmed:publicationType
Journal Article, In Vitro