Redox state of albumin is not associated with colloid osmotic pressure

Serum albumin exists in oxidized and reduced forms. Although the oxidation of albumin affects some of its functions, the relationship between oxidized albumin and colloid osmotic pressure (COP) remains unclear. The aim of this study was to determine whether there is an association between oxidized a...

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Veröffentlicht in:Molecular medicine reports 2010-07, Vol.3 (4), p.685-687
Hauptverfasser: Sakata, Masahiro, Kawaguchi, Takumi, Taniguchi, Eitaro, Nakayama, Akira, Ishizaki, Sonoko, Sonaka, Ichiro, Maganuma, Miyako, Nakamura, Toru, Itou, Minoru, Oriishi, Tetsuharu, Abe, Mitsuhiko, Yanagimoto, Chikatoshi, Koga, Hironori, Harada, Masaru, Sakamoto, Teruo, Oda, Shigeto, Sata, Michio
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Sprache:eng
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Zusammenfassung:Serum albumin exists in oxidized and reduced forms. Although the oxidation of albumin affects some of its functions, the relationship between oxidized albumin and colloid osmotic pressure (COP) remains unclear. The aim of this study was to determine whether there is an association between oxidized albumin and COP. Blood samples from 20 healthy volunteers were divided into two aliquots in order to prepare reduced (n=20) and oxidized albumin samples (n=20). This was achieved by treatment with L-cysteine and a redox-stabilizing agent before and after incubation at 37°C for 24 h. The percentage of oxidized albumin was determined by high-performance liquid chromatography. COP was measured using a colloid osmometer. Reduced and oxidized albumin samples showed 100% of reduced and 100% of oxidized albumin, respectively. There were no significant differences in albumin level and total protein level between the reduced and the oxidized albumin samples. No significant change was seen in COP between the reduced and the oxidized albumin samples (reduced albumin, 17.4±0.2 mmHg; oxidized albumin, 17.3±0.2 mmHg; P=0.465). Therefore, there is no significant difference in COP between reduced and oxidized albumin samples.
ISSN:1791-2997
1791-3004
DOI:10.3892/mmr_00000317