Chapter title |
Further characterization of DPP IV-beta, a novel cell surface expressed protein with dipeptidyl peptidase activity.
|
---|---|
Chapter number | 25 |
Book title |
Cellular Peptidases in Immune Functions and Diseases
|
Published in |
Advances in experimental medicine and biology, January 1997
|
DOI | 10.1007/978-1-4757-9613-1_25 |
Pubmed ID | |
Book ISBNs |
978-1-4757-9615-5, 978-1-4757-9613-1
|
Authors |
Julià Blanco, Etienne Jacotot, Christian Callebaut, Bernard Krust, Ara G. Hovanessian, Blanco, Julià, Jacotot, Etienne, Callebaut, Christian, Krust, Bernard, Hovanessian, Ara G. |
Abstract |
By using a CD26 negative human lymphoblastoid cell line (C8166), here we describe the characterization of a cell-surface protein which manifests CD26-like dipeptidyl peptidase IV (DPP IV) activity. This protein, referred to as DPP IV-beta, shows a higher KM value for Gly-Pro-pNA than CD26 (0.31 mM compared to 0.11 mM, respectively). In addition, DPP IV-beta was found not to bind 125I-labeled adenosine deaminase (a property of human CD26). Gel filtration experiments using extracts from C8166 and MOLT4 (a CD26 positive human T cell line) cells, revealed that the apparent molecular mass of DPP IV-beta is 82 kDa, whereas that of CD26 is 110 kDa. In order to conveniently differentiate both activities, a new family of inhibitors, that selectively blocks peptidase activity associated to CD26, has been developed. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
France | 1 | 33% |
Unknown | 2 | 67% |
Demographic breakdown
Readers by professional status | Count | As % |
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Researcher | 2 | 67% |
Other | 1 | 33% |
Readers by discipline | Count | As % |
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Agricultural and Biological Sciences | 2 | 67% |
Immunology and Microbiology | 1 | 33% |