Date of Award:

8-1972

Document Type:

Thesis

Degree Name:

Master of Science (MS)

Department:

Animal, Dairy, and Veterinary Sciences

Department name when degree awarded

Toxicology

Committee Chair(s)

R. P. Sharma

Committee

R. P. Sharma

Abstract

The association of promazine-HCl with bovine serum albumin, ammonium detergent micelles, and hemoglobin-free-rabbit-erythrocyte membranes were measured using the changes in the absorption and the emission of the interactants plus the fluorescent probe 1-anilino-8-naphthalene sulfonate. The binding of a promazine to serum protein and membrane did not alter the emission of the drug. However, the binding did produce a measurable quenching of the membrane and protein fluorescence. The quenching reaction was pH sensitive for both the protein and the membrane. Promazine binding to serum protein produced a hyperchromic change in the drugs absorption spectrum which paralleled the quenching reaction. The binding of promazine to the erythrocyte membrane was antagonized by the addition of Ca++. The promazine induced change in the fluorescent spectrum of the membrane and was dependent on the order of the addition of Ca++. Ca++ alone produced an increase in the short wavelength emission from the membrane which was interpreted as being due to an increase in tyrosine fluorescence. Carboxyl group appears to be involved in the binding of Ca++ and promazine and promazine and possibly in the quenching reaction of membrane fluorescence.

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