PREPARATION OF PHOTODYNAMIC HYDROLYSATES FROM BOVINE HEMOGLOBIN

Porphyric peptides were prepared from an agricultural byproduct, bovine hemoglobin. Hemoglobin was hydrolyzed with alcalase. After removal of heme iron, the total hydrolysate was separated on gel filtration. It consisted of three fractions; the major one was separated by reversed-phase performance chromatography. FAB analysis indicated that protoporphyrin, hematoporphyrin, and hydroxyethylvinyl deuteroporphyrin were the major porphyrin constituents. These porphyrins were maintained in solution by peptidic hydrolysates. The hydrophilic and photosensitizing properties of porphyrin-peptide complexes were demonstrated. The water-solubilizing ability of hydrolysates was significant and allowed amphiphilic porphyrins to be obtained. These compounds could give applications in different fields: they could be employed as insecticides and antibacterial products or even could give, after further purification, application in photodynamic therapy.