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Joseph A. Price, Ph.D.Joseph A. Price, Ph.D.
Professor of Pathology, Immunologist

joseph.price@okstate.edu
918.561.1441

Instructional Activities | Background | Research Interests |
Professional Interests
| Publications

Instructional Activities

  • Graduate & Medical School Immunology and Immunopathology.

Background

  • B.S. in Animal Science from Rutgers University
  • Ph.D. in Microbiology (Thesis in Mammalian Virology) from U. Massachusetts
  • Research Fellowships in Virology and Viral Oncology at Harvard and Duke Universities

Research Interests

  • Immunobiology
  • Immunodiagnostics
  • Analytical Immunochemistry

Other Professional Interests

G.R.I.P.E. (Group for Research in Pathology Education), member, member of the Technological & Software Development Committee, and Associate Editor of journal 'Pathology Education'. For more information on GRIPE, email Dr. Holliman.

Selected Publications

Buku, A., Keselman, I., Lupyan, D., Mezei, M., Price, J.A., 2008. Effective mast cell degranulating peptide inhibitors of the IgE/Fc epsilonRI receptor interaction. Chem. Biol. Drug Des. 72 (2), 133-139.

Price, J. A. 2009.  Mast cell degranulating peptides. in Bioactive Peptides, John Howl, ed. Taylor & Francis, England

Buku, A. and J. Price. 2000.  Monocyclic analogs of mast cell degranulating (MCD) peptide. Peptides 2000.  Proceedings of the 26th Euopean Peptide Symposium (J. Martinez and J. Fehrentz ed.) EDK, Paris, France. p613-614.

Buku, Angeliki; Price, Joseph A. 2001. Further studies on the structural requirements for mast cell degranulating (MCD) peptide-mediated histamine release. Peptides 22 (2001) 1987–1991.

Buku, Angeliki; Price, Joseph A.; Mendlowitz, M.; Masur, S. 2001.  Mast cell degranulating peptide binds to RBL-2H3 mast cell receptors and inhibits IgE binding. Peptides 22 (2001) 1993–1998.

Sanny, C. G., and J. A. Price. 2001. Analysis of Antibody-Antigen interactions in mixtures containing reactive and nonreactive components using size-exclusion high-performance (pressure) liquid chromatography. Analytical Biochemistry 295, 57-65.

Buku, A. , Mendlowitz, M., J.A. Price. 2002. Effects of alanine analogs of Mast Cell Degranulating (MCD) peptide on mast cell activity and binding. Peptides 2002, Proceedings of the 27th European Peptide Symposium, Sorrento, Italy.

Price, Joseph A., Sanny, C.A.  and  D. Shevlin. 2002. Inhibition of Mast Cells by Algae.  Journal of Medicinal Food, Vol. 5(4); 205-210.

Buku, A., Mendlowitz, Condie, B.A., and J.A. Price. 2003. Histamine-Releasing activity and binding to the FceRIa receptor subunit of mast cell degranulating peptide analogues with alanine substitutions. Journal of Medicinal Chemistry. 46(14):3008-12.

Sanny, C.S., Benton, R.E., and J.A. Price. 2003 Analysis of snake venom and antivenin interactions using size exclusion HPLC. Recent Research Developments in Analytical Biochemistry, 3(2003):53-60.

Buku, A., Mendlowitz, M., Condie, B.A., & Price, J.A.  2004.  Partial Alanine Scan of Mast Cell Degranulating Peptide (MCD): Importance of the Histidine and Arginine Residues.  Journal of Peptide Science, 10:313-317.

Buku, A., Condie, B.A., Price, J.A., & Mezei, M. (2005).  [Ala12]MCD peptide: a lead peptide to inhibitors of immunoglobulin E binding to mast cell receptors.  Journal of Peptide Research, 66:132-137.

Coberly, W., Price, J.A. (2005).  Analysis of Histamine Release Assays Using the Bootstrap.  Journal of Immunological Methods, 296, 103-114.

Price, J.A., Sanny, C.G., & Shevlin, D.  (2006).  Application of manual assessment of oxygen radical absorbent capacity (ORAC) for use in high throughput assay of "total" anti-oxidant activity of drugs and natural products.  Journal of Pharmacological and Toxicological Methods. 54(1): 56-61.

Price, J.A. (2007). A colorimetric assay for measuring phospholipase A2 degradation of phosphatidylcholine at physiological pH. J. Biochem. Biophys. Methods 70:441–444.

Price, J.A., and C. G. Sanny. (2007). CroFabTM  total anti-venom activity measured by SE-HPLC, and anti-PLA2 activity assayed in vitro at physiological pH. Toxicon 49:848–854.