A comprehensive account of the biochemical, toxicological, molecular, and clinical aspects of heme oxygenase, an enzyme that is important because of its function as the initial and rate-limited step in the degradation of the heme molecule. Includes an introduction to the pathway of heme metabolism, and accounts of such recent discoveries as that one of the two isozymes is a heat shock/stress protein, that bile pigments are potent antioxidants, and that synthetic metalloporphyrins control heme oxygenase activity, and hence suppress neonatal hyperbilirubinemia. A historical review traces the development of understanding since the enzyme was first described in 1968. Annotation copyright Book News, Inc. Portland, Or.
his book provides a comprehensive summary of data from basic research on characterization, regulation, and function of heme oxygenase in mammalian systems. The book also includes a major section that covers the currently used clinical methods to suppress neonatal jaundice with emphasis on the newly developed use of synthetic metalloporophyrins. This book will be welcomed by researchers and students in pharmacology, biochemistry, pharmacy, neonatology, hematology, internal medicine, and endocrinology.
