Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1992-1-23
pubmed:abstractText
Recent data from the literature have shown that cDNA clones for the carboxyterminal domain of the core protein of large proteoglycan monomers from human cartilage contain an EGF-like domain, which appears to undergo alternative splicing. In the present study we have found that articular proteoglycans from human and baboon separated on agarose flat-bed gels and blotted onto nitrocellulose react with a rabbit antiserum to mouse EGF. In addition both forms of the proteoglycans (band I and band II) seen on these gels are reactive. Reactivity is seen with proteoglycans extracted from human articular cartilage of various ages (fetal, newborn, young and aged) and with proteoglycans extracted from cartilage of thanatophoric dysplasia and homozygous achondroplasia. Reactivity is dependent on prior digestion of the nitrocellulose blot with Chase ABC, suggesting masking of epitope by chondroitin sulfate. Reactivity of the EGF antiserum with cartilage proteoglycan core protein was also demonstrated in an ELISA system with core protein as coating antigen. The reactivity appears to reside in a tryptic peptide generated from Chase/keratanase digested core protein. The immunoreactive species migrates as a 68 KDa species on gradient gels. Immunological detection and quantitative analysis of the EGF-like domain could be useful for analysis of various proteoglycan samples.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-8207
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
283-93
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Immunological detection of the EGF-like domain of the core proteins of large proteoglycans from human and baboon cartilage.
pubmed:affiliation
URA.584-CNRS, Hôpital des Enfants-Malades, Paris, France.
pubmed:publicationType
Journal Article