Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
1990-5-25
|
| pubmed:abstractText |
This paper describes the tissue distribution, purification and N-terminal amino acid sequence of the bile canalicular cell surface molecule dipeptidyl peptidase IV. Immunoperoxidase staining of cryostat sections of rat liver with a monoclonal antibody, Medical Research Council OX-61, indicated specific binding to hepatocyte bile canalicular domains and brush borders of bile ducts. Additional staining was seen in other epithelial brush borders (small intestine, kidney, colon, pancreatic duct); acinar structures in salivary glands; endothelial structures and T cell areas in thymus, spleen and lymph node. The tissue distribution suggested that monoclonal antibody OX-61 binds to the ectoenzyme dipeptidyl peptidase IV. This was confirmed by depletion of dipeptidyl peptidase IV activity from tissue homogenates by monoclonal antibody OX-61 coupled to Sepharose. The molecule recognized by OX-61 was then purified from liver and kidney by monoclonal antibody affinity chromatography. The molecule had a molecular weight of 110 kD under reducing conditions. The purified molecule was subsequently analyzed for amino acid composition and N-terminal amino acid sequence. Thirty-one N-terminal amino acids were sequenced and indicated identity with part of the predicted N-terminus of the previously cloned bile canalicular molecule GP110. On review, other similarities between dipeptidyl peptidase IV and GP110 were detected: molecular weight, deglycosylated form and metabolic half-life. Finally, the recent cloning of dipeptidyl peptidase IV permitted a comparison between the molecule recognized by monoclonal antibody OX-61, GP110 and dipeptidyl peptidase IV. It is concluded that these three molecules are almost certainly identical.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Dipeptidyl Peptidase 4,
http://linkedlifedata.com/resource/pubmed/chemical/Dipeptidyl-Peptidases and...,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0270-9139
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
11
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
534-44
|
| pubmed:dateRevised |
2010-11-18
|
| pubmed:meshHeading |
pubmed-meshheading:1970322-Amino Acid Sequence,
pubmed-meshheading:1970322-Animals,
pubmed-meshheading:1970322-Antibodies, Monoclonal,
pubmed-meshheading:1970322-Bile Canaliculi,
pubmed-meshheading:1970322-Bile Ducts,
pubmed-meshheading:1970322-Bile Ducts, Intrahepatic,
pubmed-meshheading:1970322-Blotting, Western,
pubmed-meshheading:1970322-Chromatography, Affinity,
pubmed-meshheading:1970322-Dipeptidyl Peptidase 4,
pubmed-meshheading:1970322-Dipeptidyl-Peptidases and Tripeptidyl-Peptidases,
pubmed-meshheading:1970322-Extracellular Space,
pubmed-meshheading:1970322-Immunoenzyme Techniques,
pubmed-meshheading:1970322-Liver,
pubmed-meshheading:1970322-Membrane Glycoproteins,
pubmed-meshheading:1970322-Molecular Sequence Data,
pubmed-meshheading:1970322-Molecular Weight,
pubmed-meshheading:1970322-Rats,
pubmed-meshheading:1970322-Rats, Inbred Lew
|
| pubmed:year |
1990
|
| pubmed:articleTitle |
Identification of the bile canalicular cell surface molecule GP110 as the ectopeptidase dipeptidyl peptidase IV: an analysis by tissue distribution, purification and N-terminal amino acid sequence.
|
| pubmed:affiliation |
A.W. Morrow Gastroenterology and Liver Centre, Royal Prince Alfred Hospital, Camperdown NSW, Australia.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|