Results 131 to 140 of about 20,102 (177)
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UV-trained and metal-enhanced fluorescence of biliverdin and biliverdin nanoparticles

Nanoscale, 2021
UV irradiation and metal chelation can be utilized alone or in combination to tailor the fluorescence behavior of biliverdin-based imaging probes at selected wavelengths.
Parinaz Fathi   +5 more
openaire   +2 more sources

The specificity of biliverdin reductase

BBA - Proteins and Proteomics, 1984
Maria L Tomaro   +2 more
exaly   +5 more sources

Eggshell Biliverdin as an Antioxidant Maternal Effect [PDF]

open access: yesBioEssays, 2020
AbstractIn this essay, the hypothesis that biliverdin pigment plays an antioxidant role in the avian eggshell is proposed. Due to its ability to scavenge free radical species and to reduce mutation, biliverdin potentially counteracts the oxidative action of pathogens that penetrate the eggshell and/or protects the shell membrane from oxidation, thus ...
Judith Morales
exaly   +4 more sources

Reconstitution of apomyoglobin with extended biliverdins

Biochemical and Biophysical Research Communications, 1992
An analysis of the reconstitution of biliverdins with extended conformations and horse heart apomyoglobin was carried out. Biliverdins with the 5Z-syn, 10Z-syn, 15Z-anti and 5Z-anti, 10Z-syn, 15Z-anti conformations, as well as biliverdins with the Z,Z,Z, all-syn conformation recombined with apomyoglobin.
M, Fernández   +3 more
openaire   +2 more sources

Photodecomposition of bilirubin and biliverdin in vitro

Gastroenterology, 1970
Summary Decomposition of bilirubin and biliverdin under intense fluorescent light was studied in vitro at p H levels ranging from 7.4 to 13.0. Photodecay of bilirubin was more rapid at a higher p H if albumin was absent, but more rapid at a lower p H if albumin was present, whereas biliverdin was more stable at a lower p H, with or without albumin.
J D, Ostrow, R V, Branham
openaire   +2 more sources

Biliverdin pigments in green biles

Biochimica et Biophysica Acta (BBA) - General Subjects, 1965
Abstract 1. 1. The nature of the green bile pigments in various animal species has been studied using reversed-phase partition chromatography and paper chromatography. 2. 2. The chromatographic behaviour of the pigments has been compared with that of synthetic biliverdin derivatives. 3. 3.
E R, GARAY, B, NOIR, M, ROYER
openaire   +2 more sources

Separation and properties of conjugated biliverdin

Biochimica et Biophysica Acta (BBA) - General Subjects, 1965
Abstract 1. 1. Reversed-phase partition chromatography and paper chromatography have been used to separate free biliverdin from conjugated biliverdin. 2. 2. The colour of green post-mortem bile appears to be associated with both biliverdin monoglucuronide and biliverdin diglucuronide. 3. 3.
B A, NOIR, E R, GARAY, M, ROYER
openaire   +2 more sources

THE SINGLET OXYGEN REACTIVITY OF BILIVERDIN

Photochemistry and Photobiology, 1977
Abstract— In 1, 1, 2‐trichlorotrifluoroethane solution biliverdin physically quenches singlet oxygen at a rate of 8 × l0sM‐1s‐1 and reacts chemically at 6 × 10 5M‐1s‐1 to give a red product. In D, O solution the rate constants are PD dependent and range from 1.5–6 times 1010M‐1s‐1 for quenching and the chemical rate varies from 3–5 × 108 M‐1 s‐1 to ...
I B, Matheson, M M, Toledo
openaire   +2 more sources

THE TRIPLET EXCITED STATES OF BILIVERDIN AND BILIVERDIN DIMETHYL ESTER

Photochemistry and Photobiology, 1979
Abstract— The triplet states of biliverdin and biliverdin dimethyl ester have been generated using pulse radiolysis excitation. Biliverdin triplet was formed by energy transfer from biphenyl triplet in acetone, absorbed throughout the wavelength range studied (380–1000 nm) and had a half‐life of 11.7μs under the cpnditions chosen.
openaire   +1 more source

The specificity of biliverdin reductase. A study with different biliverdin types.

Biochimica et biophysica acta, 1985
The 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
openaire   +1 more source

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