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Tropical Journal of Pharmaceutical Research
Pharmacotherapy Group, Faculty of Pharmacy, University of Benin, Benin City, Nigeria
ISSN: 1596-5996
EISSN: 1596-9827
Vol. 13, No. 6, 2014, pp. 855-862
Bioline Code: pr14120
Full paper language: English
Document type: Research Article
Document available free of charge

Tropical Journal of Pharmaceutical Research, Vol. 13, No. 6, 2014, pp. 855-862

 en Expression and Purification of Soluble, Biologically Active Recombinant Dipeptidyl Peptidase 4 (DPP4/CD26/ADAbp) Comprising the Extracellular Domain in the Yeast, Pichia pastoris check for this species in other resources
Kang, Hyun

Abstract


Purpose: To investigate Pichia pastoris check for this species in other resources expression system for producing clinically usable, high-quality dipeptidyl peptidase 4 recombinant protein.
Methods: The yeast, Pichia pastoris, expression system was used for the production of the human recombinant dipeptidyl peptidase 4 as a secreted form. The full-length human dipeptidyl peptidase 4 corresponding to the amino acid 31-766 was subcloned into a Pichia pastoris expression vector, pPICZ􏰓, and transformed to Pichia pastoris X33 cells.
Results: The human recombinant dipeptidyl peptidase 4 protein was expressed enzymatically as active human rDPP4(31-766) as secreted form in the yeast P. pastoris, purified and monitored its biological activity. The test DPP4 recombinant protein induced a significant increase of DDP4 activity at 10, 20 and 30 min incubation time (p < 0.05) and at 40 min (p < 0.001). A similar pattern was found for the commercial (standard) DPP4 protein at 10, 20 and 30 min (p < 0.05) and at 40 min (p < 0.001). The high standard deviation (SD) associated with the mean value for the DPP4 activity is due to incubation time sometimes associated with high DPP4 values. The values were much higher than in other groups as expected.
Conclusion: Human recombinant dipeptidyl peptidase 4(31-766) protein in the yeast Pichia pastoris, obtained using the technique employed in this study can further improve production efficiency and costs of human recombinant dipeptidyl peptidase 4 and other recombinant proteins.

Keywords
DPP4; Pichia pastoris; Recombinant protein; Expression; Purification

 
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