Studies of Oxidant-Induced Changes in Albumin Transport Function with a Fluorescent Probe K-35. Metal-Catalyzed Oxidation

Aseychev, A. V.; Азизова, О. А.; Beckman, E. M.; Skotnikova, O. I.; Piryazev, A. P.; Dobretsov, G. E.

doi:10.1007/s10517-012-1741-5

Cited by 2 publications

(1 citation statement)

References 8 publications

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“…The assay is based on its specific interaction of albumin with the fluorescent probe K-35 (N-(carboxyphenyl)imide of 4-(dimethylamino)naphthalic acid, synthesized in the Federal Research and Clinical Center of Physicochemical Medicine, Ministry of Health of the Russian Federation) [ 66 , 67 , 68 , 69 , 70 ]. The reaction with K-35 allows for selective study of changes in drug site II in the albumin molecule next to which the tryptophan residue is localized.…”

Section: Methodsmentioning

confidence: 99%

Effect of Low-Dose Line-Spectrum and Full-Spectrum UV on Major Humoral Components of Human Blood

Sozarukova,

Skachko,

Chilikina

et al. 2023

Molecules

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Ultraviolet blood irradiation (UVBI) is an alternative approach to the treatment of infectious diseases of various pathogeneses. Recently, UVBI has attracted particular interest as a new immunomodulatory method. Experimental studies available in the literature demonstrate the absence of precise mechanisms of the effect of ultraviolet radiation (UV) on blood. Here, we investigated the effect of UV radiation of line-spectrum mercury lamp (doses up to 500 mJ/cm2) traditionally used in UVBI on the major humoral blood components: albumin, globulins and uric acid. Preliminary data on the effect of various doses of UV radiation of full-spectrum flash xenon lamp (doses up to 136 mJ/cm2), a new promising source for UVBI, on the major blood plasma protein, albumin, are presented. The research methodology included spectrofluorimetric analysis of the oxidative modification of proteins and analysis of the antioxidant activity of humoral blood components by chemiluminometry. The effect of UV radiation on albumin caused its oxidative modification and, accordingly, an impairment of the transport properties of the protein. At the same time, UV-modified albumin and γ-globulins acquired pronounced antioxidant properties compared to native samples. Uric acid mixed with albumin did not protect the protein against UV-induced oxidation. The flash full-spectrum UV qualitatively had the same effect on albumin as line-spectrum UV did, but an order of magnitude lower doses were required to achieve comparable effects. The suggested protocol can be used for selecting a safe individual dose for UV therapy.

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Section: Methodsmentioning

confidence: 99%

Effect of Low-Dose Line-Spectrum and Full-Spectrum UV on Major Humoral Components of Human Blood

Sozarukova,

Skachko,

Chilikina

et al. 2023

Molecules

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Effect of Oxidatively Modified and Non-Modified Human Serum Albumin on Luminol-Dependent Chemiluminescence of Human Peripheral Blood Leukocytes Stimulated with Opsonized Zymosan

et al. 2014

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We studied the effects of native and oxidized human serum albumin on luminol-dependent chemiluminescence of human peripheral blood leukocytes stimulated with opsonized zymosan. Human serum albumin was added simultaneously with opsonized zymosan at the beginning of the chemiluminescent reaction. Otherwise, leukocytes were incubated with human serum albumin at 37°C for various periods before addition of opsonized zymosan. Oxidized human serum albumin was obtained by the method of metal-catalyzed oxidation. In control to non-modified albumin, oxidized albumin produced an inhibitory effect on luminol-dependent chemiluminescence of leukocytes. These changes were observed in experiments with addition of oxidized albumin at the beginning of a chemiluminescent reaction and after incubation of study agent with cells.

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Studies of Oxidant-Induced Changes in Albumin Transport Function with a Fluorescent Probe K-35. Metal-Catalyzed Oxidation

Cited by 2 publications

References 8 publications

Effect of Low-Dose Line-Spectrum and Full-Spectrum UV on Major Humoral Components of Human Blood

Effect of Low-Dose Line-Spectrum and Full-Spectrum UV on Major Humoral Components of Human Blood

Effect of Oxidatively Modified and Non-Modified Human Serum Albumin on Luminol-Dependent Chemiluminescence of Human Peripheral Blood Leukocytes Stimulated with Opsonized Zymosan

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