Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1989-11-13
pubmed:abstractText
A monoclonal antibody (mAb) specific for human recombinant IL-1 beta (hu rIL-1 beta) was produced by immunizing BALB/c mice with hu rIL-1 beta purified with classical methods. This mAb recognizes an epitope within the highly hydrophylic fragment spanning amino acid 133-147. The affinity constant of this mAb towards IL-1 beta was determined by RIA. An affinity column was prepared by covalent binding of the mAb to Sepharose CL-4B. The column was capable of selectively binding hu rIL-1 beta produced in Escherichia coli directly from crude homogenates. The IL-1 beta protein yield was higher than 90% with a very good recovery of IL-1 beta biological activity. Moreover, the immunosorbent retained at least two thirds of its IL-1 beta-binding capacity after 20 cycles of purification.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0022-1759
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
123
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-8
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
One-step immunoaffinity purification of bioactive human recombinant IL-1 beta with a monoclonal antibody directed to a well-exposed domain of the protein.
pubmed:affiliation
Sclavo Research Center, Siena, Italy.
pubmed:publicationType
Journal Article