Results 101 to 110 of about 183 (125)
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The specificity of biliverdin reductase. The reduction of biliverdin XIII isomers.

Biochimica et biophysica acta, 1984
The substrate specificity of the different molecular forms of biliverdin reductase (bilirubin:NAD(P)+ oxidoreductase, EC 1.3.1.24) using biliverdin XIII alpha, XIII beta and XIII gamma was examined. It was found that molecular form 1 (the major form in normal rat liver) reduced biliverdin XIII alpha at a much higher rate than the other two isomers ...
J, Awruch   +3 more
openaire   +1 more source

Confirmation of the assignment of human biliverdin reductase to chromosome 7

Annals of Human Genetics, 1984
SummarySegregation 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
openaire   +2 more sources

Biliverdin reductase activity in cattle, sheep, rabbits and rats

International Journal of Biochemistry, 1989
1. 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
openaire   +2 more sources

Evidences of Biological Functions of Biliverdin Reductase A in the Bovine Epididymis

Journal of Cellular Physiology, 2015
Epididymal 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
openaire   +2 more sources

Affinity Chromatography of Biliverdin Reductase

Biochemical Society Transactions, 1976
WATT, JANE, O'CARRA, PÁDRAIG
openaire   +2 more sources

Crystal structure of rat biliverdin reductase.

Nature structural biology, 2001
Biliverdin reductase (BVR) is a soluble cytoplasmic enzyme that catalyzes the conversion of biliverdin to bilirubin using NADH or NADPH as electron donor. Bilirubin is a significant biological antioxidant, but it is also neurotoxic and the cause of kernicterus. In this study, we have determined the crystal structure of rat BVR at 1.4 A resolution.
A, Kikuchi   +6 more
openaire   +1 more source

The heme oxygenase/biliverdin reductase system in skin cancers.

Journal of biological regulators and homeostatic agents, 2015
The heme oxygenase/biliverdin reductase (HO/BVR) pathway enhances cell stress response by degrading excess heme or producing antioxidant and cytoprotective molecules. Recently, members of the HO/BVR system have been proposed as biomarkers for the early diagnosis of free radical-related diseases.
Arena, Vincenzo   +3 more
openaire   +2 more sources

Biliverdin reductase

1993
Dietmar Schomburg   +2 more
openaire   +1 more source

Biliverdin Reductase A is a major determinant of neuroprotective Nrf2 signaling

Abstract Biliverdin reductase A (BVRA), the terminal enzyme in heme catabolism, generates the neuroprotective and lipophilic antioxidant bilirubin. Here, we identify a novel non-enzymatic role for BVRA in redox regulation. We show that BVRA directly interacts with nuclear factor erythroid-derived factor-like 2 (Nrf2), the master ...
Chirag, Vasavda   +20 more
openaire   +2 more sources

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