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ENCAPSULATION OF THE THROMBOLYTIC ENZYME, BRINASE, IN PHOTOSENSITIZED ERYTHROCYTES - A NOVEL THROMBOLYTIC SYSTEM BASED ON PHOTODYNAMIC ACTIVATION

Biomedical Sciences Research Institute Computer Science Research Institute Environmental Sciences Research Institute Nanotechnology & Advanced Materials Research Institute

FLYNN, G, HACKETT, TJ, MCHALE, L and MCHALE, AP (1994) ENCAPSULATION OF THE THROMBOLYTIC ENZYME, BRINASE, IN PHOTOSENSITIZED ERYTHROCYTES - A NOVEL THROMBOLYTIC SYSTEM BASED ON PHOTODYNAMIC ACTIVATION. JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY, 26 (2). pp. 193-196. [Journal article]

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DOI: 10.1016/1011-1344(94)07037-7

Abstract

In order to circumvent many of the problems associated with the systemic administration of agents used in thrombolytic therapy, it was decided to investigate the possibility of using erythrocytes as carriers and delivery vehicles for these agents. The enzyme brinase, a fibrinolytic enzyme produced by Aspergillus oryzae, was loaded into rabbit erythrocytes using electroporation. The loading index for this enzyme was found to be 60% and incorporation appeared to be relatively stable over a period of 4 h. In order to facilitate the predetermined release of the loaded component from the erythrocytes, they were photosensitized using haematoporphyrin derivative (HPD) and release was demonstrated within 5 min of photoactivation. Inclusion of the loaded, photosensitized system into clotting blood and subsequent exposure to light demonstrated almost complete lysis of the clot. We believe that this system exhibits potential for use in thrombolytic therapy.

Item Type:Journal article
Faculties and Schools:Faculty of Life and Health Sciences
Faculty of Life and Health Sciences > School of Pharmacy and Pharmaceutical Science
Research Institutes and Groups:Biomedical Sciences Research Institute
Biomedical Sciences Research Institute > Pharmaceutical Science and Practice
ID Code:21511
Deposited By:Professor Anthony McHale
Deposited On:28 Mar 2012 16:10
Last Modified:04 Dec 2012 11:59

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