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Structural Biological Study of Biliverdin Reductase.
Nihon Kessho Gakkaishi, 2001 openaire +2 more sources
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Biliverdin reductase: substrate specificity and kinetics
BBA - Proteins and Proteomics, 1987The substrate specificity of the different forms of rat liver biliverdin reductase was examined using synthetic biliverdins. Biliverdins carrying methyl, ethyl and one propionate residue in their structure were not substrates of biliverdin reductase. Biliverdins with one propionate and one acetate residue or with two acetate residues were not reduced ...
Rosalia B Frydman +2 more
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Overexpression of biliverdin reductase enhances resistance to chemotherapeutics
Cancer Letters, 2011Biliverdin reductase (BVR) converts biliverdin to bilirubin. Additionally, acting as a transcription factor and possessing a capacity of a serine/threonine kinase, it may modulate signaling pathways. In order to gain better understanding of BVR functions, we used genetically modified line of mouse fibroblasts with reversible overexpression of BVR ...
Urszula Florczyk +2 more
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The reaction mechanism of bovine kidney biliverdin reductase
BBA - Proteins and Proteomics, 1988The steady-state kinetics of biliverdin reductase can be studied in detail at pH 9 as under these conditions the Km for biliverdin is high enough to obtain reliable measurements of the initial rate in the absence of any biliverdin binding proteins. The initial rate kinetics and the product-inhibition studies are consistent with an ordered sequential ...
Timothy J Mantle, T J Mantle
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The specificity of biliverdin reductase
BBA - Proteins and Proteomics, 1984Maria L Tomaro +2 more
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Detection of Biliverdin Reductase Activity
Current Protocols in Toxicology, 1999AbstractThe conversion of biliverdin to the bile pigment bilirubin is catalyzed by biliverdin reductase, a cytosolic enzyme with two pH optima with different cofactors. The enzyme is assayed at pH 8.7 with NADPH as a cofactor and at 6.75 with NADH. The production of bilirubin is detected as described in this unit with a spectrophotometric assay.
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Kinetic properties and regulation of biliverdin reductase
Archives of Biochemistry and Biophysics, 1988In kinetic studies of the dual nucleotide enzyme biliverdin reductase, product inhibition patterns obtained with bilirubin as the inhibitor, using either the NADPH-linked reaction at pH 8.7 or the NADH-linked reaction at pH 7.0, are consistent with a random order of substrate addition and product release at either pH.
J E, Bell, M D, Maines
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Purification and Properties of Cow Splenic Biliverdin Reductase
Preparative Biochemistry, 1994Biliverdin reductase was purified from cow spleen. The specific activity of the final enzyme preparation was 24.01 u/mg, representing 686-fold purification as measured with NADPH. The yield was 3 grams of enzyme per 100 grams of cow spleen. The purified enzyme was a monomeric protein with an apparent molecular weight of about 34,000 and an isoelectric ...
Z, Ding, Y, Xu
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PURIFICATION AND PROPERTIES OF SALMON LIVER BILIVERDIN REDUCTASE
Biochemical Society Transactions, 1995Biliverdin reductase (BVR: bilirubin:NAD(P)+ oxidoreductase; EC 1.3.1.24) is responsible for the conversion of biliverdin to bilirubin a t the end of the haem catabolic pathway. Elevated levels of serum bilirubin (hyperbilirubinaemia) occur when bilirubin conjugation is impaired.
G, Elliott, T J, Mantle
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The specificity of biliverdin reductase. A study with different biliverdin types.
Biochimica et biophysica acta, 1985The specificity of rat liver biliverdin reductase was examined with the help of a series of synthetic biliverdins. The mixture of the four biliverdin isomers obtained by the chemical oxidation of protohemin I, protohemin XI, protohemin XIV and harderohemin were used as substrates of biliverdin reductase and were compared with the mixture of biliverdins
M L, Tomaro +6 more
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