Dr. Randall A. Kopper

Randall Kopper

Professor of Chemistry
Nancy and Craig Wood Odyssey Professor

Office: Acxiom Hall 205
Phone: (501) 450-1275
Fax: (501) 450-3829
E-mail: kopper@hendrix.edu 
  • Postdoctoral Fellow, University of Missouri-Columbia
  • Ph.D., University of Kansas
  • B.A., Monmouth College
 

Teaching Experience

  • Professor of Chemistry, Hendrix College, 1983 to present
  • Nancy and Craig Wood Odyssey Professor of Chemistry, 2011 to present

Research Interests

  • Analysis and characterization of snake venom enzymes
  • Isolation, purification, and characterization of peanut protein allergens
  • Development of treatments for peanut allergy

Recent Publications

  • Kopper RA, Van T, Kim A, Helm RM. Release of Soluble Protein from Peanut (Arachis hypogaea, Leguminosae) and Its Adsorption by Activated Charcoal. Journal of Agricultural and Food Chemistry 2011; 59: 236-240.
  • Kopper RA, Kim A, Van T, Helm RM.  Adsorption of Peanut (Arachis hypogaea, Leguminosae) Proteins by Activated Charcoal. Journal of Agricultural and Food Chemistry 2008; 56: 10619-10624.
  • Kopper RA, West CM, Helm RM. Comparison of physiological and in vitro porcine gastric fluid digestion. International Archives of Allergy and Immunology 2006; 141: 217-222.
  • Kopper RA, Odum NJ, Sen M, Helm RM, Stanley JS, Burks AW. Peanut protein allergens: The effect of roasting on solubility and allergenicity. International Archives of Allergy and Immunology 2005; 136: 16-22.
  • Kopper RA, Odum NJ, Sen M, Helm RM, Stanley JS, Burks AW. Peanut protein allergens: Gastric digestion is carried out exclusively by pepsin. Journal of Allergy and Clinical Immunology 2004; 114: 614-618.
  • Sen M, Kopper R, Pons L, Abraham EC, Burks AW, Bannon GA. Protein structure plays a critical role in peanut allergen stability and may determine immunodominant IgE-binding epitopes. Journal of Immunology 2002; 169: 882-887.
  • Maleki SJ, Kopper RA, Shin DS, Park CW, Compadre CM, Sampson H, Burks AW, Bannon GA. Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation. Journal of Immunology 2000; 164: 5844-5849.