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Mechanism of proline-specific proteinases: (I) Substrate specificity of dipeptidyl peptidase IV from pig kidney and proline-specific endopeptidase from Flavobacterium meningosepticum.
Dipeptidyl peptidase IV in the immune system. Effects of specific enzyme inhibitors on activity of dipeptidyl peptidase IV and proliferation of human lymphocytes.
New active site-specific peptide inhibitors for their efficiency as inhibitors of lymphocyte DP IV and DNA synthesis of mitogen-stimulated lymphocytes are tested, yielding half-maximal inhibitory concentrations in the micromolar range.
[Catalytic mechanism of dipeptidyl-peptidase IV].
Kinetic studies involving two competing substrates suggest the probable existence of a catalytic centre for both groups of substrates and the existence of an acyl-enzyme mechanism is considered likely.
The role of dipeptidyl peptidase IV in human T lymphocyte activation. Inhibitors and antibodies against dipeptidyl peptidase IV suppress lymphocyte proliferation and immunoglobulin synthesis in vitro
DP IV, an ectoenzyme in the cell membrane of T lymphocytes, is an important constituent in the process of lymphocyte activation and as a consequence of impaired T cell function the production of immunoglobulins by pokeweed mitogen‐stimulated lymphocytes is also markedly reduced in the presence of DP IV inhibitors.
The conformation around the peptide bond between the P1- and P2-positions is important for catalytic activity of some proline-specific proteases.
A clinical physiologic study of hydroxyethyl starch.
Dipeptidyl Peptidase IV in Human T Lymphocytes
It is suggested that the membrane peptidase DP IV is involved in the induction and activation of cytokines controlling lymphocyte proliferation.
Dipeptidyl-peptidase IV-beta, a novel form of cell-surface-expressed protein with dipeptidyl-peptidase IV activity.
- E. Jacotot, C. Callebaut, A. Hovanessian
- Biology, ChemistryEuropean journal of biochemistry
- 1 July 1996
The results suggest that DPP IV-beta is a CD26-like protein which could be characterized by distinct properties.
Derivatives of β-casomorphins with high analgesic potency
Extended investigation of the substrate specificity of dipeptidyl peptidase IV from pig kidney.
- J. Rahfeld, M. Schutkowski, J. Faust, K. Neubert, A. Barth, J. Heins
- Biology, ChemistryBiological chemistry Hoppe-Seyler
- 1 May 1991
The substrate specificity of dipeptidyl peptidase IV from pig kidney was investigated, using a series of substrates, in which the amino-acid residue in position P1, a structural derivative of proline, was altered with respect to ring size and substituents.