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Sulfur Transferases and Cyanide Pretreatment.
Annual rept. 15 Jun 84-14 Jun 85,
TEXAS A AND M UNIV COLLEGE STATION DEPT OF MEDICAL PHARMACOLOGY AND TOXICOLOGY
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The predominant mechanism for detoxifying cyanide is to interact cyanide with a sulfur donor, sodium thiosulfate, in the presence of sulfur transferase called rhodanese Rh. This enzyme is present in the body in large concentrations, has a high turnover number of 20,000, one molecule of enzyme can metabolize 20,000 molecules of cyanide per minute, and this reaction is irreversible. Most of the initial first year was spent on attempting to isolate and crystallize this enzyme from beef liver in preparative amounts. This research is concerned with investigating the biochemical and pharmacological properties of the sulfur transferase enzymes in cyanide pretreatment. The enzyme is being encapsulated in erythrocytes with sodium thiosulfate and the toxicologic properties of these procedures are being investigated. Author
APPROVED FOR PUBLIC RELEASE