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The Use of Synthetic Linear Tetrapyrroles to Probe the Verdin Sites of Human Biliverdin-IXα Reductase and Human Biliverdin-IXβ Reductase [PDF]
FEBS Journal, 2009 Many vertebrate species express two enzymes that are capable of catalysing the reduction of various isomers of biliverdin. Biliverdin‐IXα reductase (BVR‐A) is most active with its physiological substrate biliverdin‐IXα, but can also reduce the three other biliverdin isomers IXβ, IXδ and IXγ.
Mostafa A S Hammam +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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Evidences of Biological Functions of Biliverdin Reductase A in the Bovine Epididymis
Journal of Cellular Physiology, 2015Epididymal sperm binding protein 1 (ELSPBP1) is secreted by the epididymal epithelium via epididymosomes and is specifically transferred to dead spermatozoa during epididymal transit. We identified biliverdin reductase A (BLVRA) as a partner of ELSPBP1 by immunoprecipitation followed by tandem mass spectrometry.
Olivier, D'Amours +5 more
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Confirmation of the assignment of human biliverdin reductase to chromosome 7
Annals of Human Genetics, 1984SummarySegregation of biliverdin reductase (BLVR) in 11 independent human‐mouse hybrids confirms the assignment to chromosome 7 in man and gives a regional localization of 7pter → 7q22. Isoelectric focusing of BLVR reveals genetically determined variation among inbred strains of mice.
M, Parkar +6 more
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Biliverdin reductase activity in cattle, sheep, rabbits and rats
International Journal of Biochemistry, 19891. Biliverdin reductase (BVR) activity was measured in post-microsomal supernatants of livers of cattle, sheep, rabbits and rats. BVR activities in bovine and ovine livers were 4.7 and 5.0%, respectively, of rat liver activity. 2. The finding of BVR activity in ruminants is in contrast to a previous report and may be due to the use of a different assay
J W, George +4 more
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Affinity Chromatography of Biliverdin Reductase
Biochemical Society Transactions, 1976WATT, JANE, O'CARRA, PÁDRAIG
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