HPLC‐studies on nonmercapt‐mercapt conversion of human serum albumin

Sogami, Masaru; Era, Seiichi; Nagaoka, Shunji; Kuwata, Kazuo; Kida, Kimihiro; Miura, Kiyoshi; Inouye, Hiroshi; Suzuki, Eiji; Hayano, Shigeo; Shibata, Shigeki

doi:10.1111/j.1399-3011.1985.tb02191.x

Cited by 61 publications

(30 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…HNA has a reversibly oxidized form (HNA-1) and a strongly oxidized form (HNA-2), which accounts for a very small fraction of the total HNA. Although total HNA constitutes 20-25% of plasma albumin in healthy subjects, 19,20 our patients showed significantly higher percentages of HNA (HNA-1 and HNA-2) on starting HD; this result is similar to the findings of previous reports. 17,20 In this crossover study, however, there were no significant differences between the results before and after EVAL treatment and between the results before and after CTA treatment (Figure 1).…”

Section: Plasma Predialysis Hna Proportions Did Not Improve With 2 Mosupporting

confidence: 91%

“…The major HNA is the disulfide bonding form, which reversibly oxidizes the mercapto group by either cysteine or glutathione, according to the level of the surrounding oxidative stress. 19 In earlier reports, the HNA fraction of serum albumin decreased transiently in all HD patients after a single HD session, which was demonstrated by HPLC profiles. 19,28 Furthermore, a recent study on peritoneal dialysis patients showed that their HNA proportions correlated significantly with serum urea nitrogen but not with other variables considered.…”

Section: Discussionmentioning

confidence: 71%

See 1 more Smart Citation

Ethylene-Vinyl Alcohol Copolymer Dialyzer Membrane Reduces Protein Oxidation in Hemodialysis Patients

Matsumoto

Mukai

Arihara³

et al. 2011

Renal Failure

View full text Add to dashboard Cite

Background: Oxidative stress has been implicated in the cardiovascular complications that affect hemodialysis (HD) patients. Ethylene-vinyl alcohol copolymer (EVAL) dialyzer membrane induces less production of reactive oxygen species as compared to conventional dialyzers. We evaluated the impact of EVAL membrane on plasma protein oxidation in HD patients. Methods: HD patients treated with cellulose triacetate (CTA) dialyzers were selected. In the first study performed in a 2-month crossover design alternating between CTA and EVAL, nonmercaptalbumin and advanced oxidation protein products levels were measured in the predialysis blood from 10 subjects. In the second study, predialysis plasma myeloperoxidase levels were measured before and after a 2-week EVAL treatment on 12 patients. Results: Plasma advanced oxidation protein products levels were reduced after a 2-month EVAL treatment and increased again after CTA treatment, although the nonmercaptalbumin proportions were not affected significantly by the change in dialyzer membranes. The following study, a 2-week EVAL treatment, showed the decrease in myeloperoxidase levels immediately before HD. Conclusion: The frequent use of EVAL dialyzers has been shown to reduce protein oxidation, possibly through the suppression of circulating phagocytes. This novel biocompatible dialyzer is expected to protect cardiovascular mortality in HD patients.

show abstract

Section: Plasma Predialysis Hna Proportions Did Not Improve With 2 Mosupporting

confidence: 91%

Section: Discussionmentioning

confidence: 71%

Ethylene-Vinyl Alcohol Copolymer Dialyzer Membrane Reduces Protein Oxidation in Hemodialysis Patients

Matsumoto

Mukai

Arihara³

et al. 2011

Renal Failure

View full text Add to dashboard Cite

show abstract

“…This has been demonstrated by high-performance liquid chromatographic (HPlc) analysis (7). in healthy adults, approximately 75% of the cys-34 molecules in albumin contain a free sulfhydryl group (reduced albumin), while approximately 25% (oxidized albumin) form a disulfide with small sulfhydryl compounds, such as another cysteine, homocysteine or glutathione (8).…”

Section: Introductionmentioning

confidence: 99%

Redox state of albumin is not associated with colloid osmotic pressure

Sakata

Kawaguchi²,

Taniguchi³

et al. 2010

Mol Med Rep

View full text Add to dashboard Cite

Abstract. 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.

show abstract

“…Human serum albumin (HSA) is composed of mercaptalbumin (HMA) with a free thiol group 2 on Cys-34, nonmercaptalbumin 1 (HNA1) with Cys-34 bound to cystein or glutathione by a 3 disulfide bond, and nonmercaptalbumin 2 (very small amount) with Cys-34 oxidized to sulfenic, 4 sulfinic or sulfonic [1][2][3][4]. HMA is the major extracellular source of reduced sulfhydryl groups, 5 which are potent scavengers of reactive oxygen and nitrogen species [8].…”

mentioning

confidence: 99%

“…Oxidative stress is believed to play a major role in the pathogenesis of 8 several diseases [5][6][7]. Therefore, in order to observe the redox state of circulatory system, HMA 9 and HNA were extensively determined in serum or other biological fluids of the elderly and the 10 patients with renal and liver dysfunctions, endocrine diseases, eye diseases [1,[9][10][11][12][13][14][15][16]. 11 Several HPLC methods with ultraviolet (UV) or fluorescence (FL) detection were developed 12 for the determination of HMA and HNA1 [9, 10, 13-17].…”

mentioning

confidence: 99%