• Journal of the Korean Society of Food Science and Nutrition
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• v.23 no.3
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• pp.414-419
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• 1994

This study was trying to find what physical changes occurred to albumin when it reacted with estrogen and other ligands. Each concentration of human serum albumin with 100$\mu$l estradiol reacted at the highest binding capacity of 280nm. In addition, 1 hr of reaction time showed the highest binding rate. Conformational changes in human serum albumin with dietylstillbesterol and N-ethyl-maleimide produced strong binding capacities. The changes were immediate and they did not increase or decrease over time. Effects of human serum albumin with estriol induced no interaction each other. The binding capacity of human serum albumin with vitamin D$_2$was lower than estradiol. and the highest binding rate showed 1 hr of reaction time. Vitamin D$_2$ was very similar to the binding capacity of estradiol.

• Applied Biological Chemistry
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• v.1
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• pp.48-54
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• 1960

Studing the binding of the 5-Iodopyrimdines by human serum albumin we obtained the following conclusions; 1. The more strong electron donating groups in the molecule of 5-Iodopyrimidines, the larger the binding force with human serum albumin. This trend seems to be attributed by increase of polarization of the electron donating groups in 5-Iodopyrimidines molecule. 2. The binding force of 5-Iodopyrimidines by human serum albumin is increased with the pH increasing could be occurred the configurational changes of human albumin molecule, and this new binding sites of human serum albumin molecule would form the intermolecular complex with 5-Iodopyrimidines molecule more strongly.

• YAKHAK HOEJI
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• v.25 no.4
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• pp.161-165
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• 1981

The binding of two cephalosporins, cephalothin and cefazoline to human serum albumin(HSA) was studied by difference spectrophotometry using a spectrophotometric probe, 2-(4'-hydroxybenzeneazo) benzoic acid. The probe is strong visible absorbing material which interacts with serum albumin to give characteristic spectrophotometric peaks and provides the basis for a convenient assay to measure free and bound amounts in the presence of serum albumin and competitive drugs. The results obtained showed that the probe and cephalosporin compete for the same binding site on human serum albumin; thus the probe can be used to gauge the displacement of cephalosporins from human serum albumin. The data were interpreted on the basis of theory of multiple equilibria. The number of binding sites of human serum albumin for 2-(4'-hydroxybenzeneazo) benzoic acid(HBAB), cephalothin and cefazoline appears to be 4. By using this technique the binding constants were found as follows: HSA-HBAB, $7.89{\times}10^{4}M^{-1}$; HSA-cephalothin, $1.09{\times}10^{3}M^{-1}$ ; HSA-cefazoline, $1.21{\times}10^{3}M^{-1}$.

• Journal of Preventive Medicine and Public Health
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• v.45 no.2
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• pp.98-104
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• 2012

Objectives: A positive association between serum albumin levels and metabolic syndrome has been reported in observation studies, but it has not been established in the Korean population. The purpose of this study was to evaluate the association between serum albumin levels and the presence of metabolic syndrome among a sample of apparently healthy Korean adults. Methods: This cross-sectional study analyzed data of 3189 community-dwelling people (1189 men and 2000 women) who were aged 40 to 87 years and were living in a rural area in Korea. Serum albumin levels were classified into quartile groups for each sex. Metabolic syndrome was defined according to the National Cholesterol Education Program Adult Treatment Panel III guidelines with an adjusted waist circumference cut-off value ${\geq}90\;cm$ for men and${\geq}85\;cm$ for women). An independent association between serum albumin levels and metabolic syndrome was assessed by multiple logistic regression analysis. Results: Higher serum albumin levels were associated with increased prevalence of metabolic syndrome. The odds ratio (95% confidence interval) of the prevalence of metabolic syndrome for the highest versus the lowest serum albumin quartiles was 2.81 (1.91 to 4.14) in men and 1.96 (1.52 to 2.52) in women, after adjusting for age, smoking status, alcohol consumption, and physical activity. When each metabolic abnormality was analyzed separately, higher serum albumin levels were significantly associated with hypertriglyceridemia and hyperglycemia in both sexes, and with abdominal obesity in men. Conclusions: These results suggest that higher serum albumin levels are positively associated with an increased risk of metabolic syndrome in Korean adults.

• Journal of Photoscience
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• v.12 no.1
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• pp.11-15
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• 2005

The mechanism of interaction of two drugs viz., amoxicillin and cloxacillin with bovine serum albumin has been investigated using fluorescence absorption and circular dichroism spectroscopy. The quenching mechanism of fluorescence of bovine serum albumin by amoxicillin and cloxacillin was discussed. The binding sites number n and apparent binding constant Kwere measured by fluorescence quenching method. The thermodynamic parameters obtained from data at different temperatures were calculated. The distance r between donor (bovine serum albumin) and acceptor (amoxicillin and cloxacillin) was obtained according to Forster theory of non-radiative energy transfer. The effect of common ions on binding constant was also investigated. The results of synchronous fluorescence spectra, UV-vis absorption spectra and circular dichroism of BSA in presence of amoxicillin and cloxacillin show that the conformation of bovine serum albumin changed

• Nutrition Research and Practice
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• v.11 no.1
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• pp.57-63
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• 2017

BACKGROUND/OBJECTIVES: The level of serum albumin is an index of nourishment care and management. However, the distribution and correlates of serum albumin levels among individuals with motor disorders have not been reported until now. Therefore, we examined the distribution and correlates of serum albumin levels among individuals with motor disorders. SUBJECTS/METHODS: A cross-sectional study on 249 individuals with motor disabilities (144 men, mean age: 51.4 years; 105 women, mean age: 51.4 years) was conducted at five institutions in Ibaraki Prefecture, Japan in 2008. The results were compared with data from the National Health and Nutrition Survey. RESULTS: The mean serum albumin levels were $4.0{\pm}0.4g/dL$ for men and $3.8{\pm}0.5g/dL$ for women. Overall, 17 (11.8%) men and 25 (23.8%) women had hypoalbuminemia (serum albumin level ${\leq}3.5g/dL$); these proportions were greater than those among healthy Japanese adults (${\leq}1%$). Low serum albumin level was related with female sex, older age, low calf circumference, low relative daily energy intake, low hemoglobin (Hb), low blood platelet count, low high-density lipoprotein cholesterol (HDL-C), low $HbA_{1c}$, and high C-reactive protein (CRP) levels. The strongest correlates, based on standardized betas, were Hb (0.321), CRP (-0.279), and HDL-C (0.279) levels. CONCLUSIONS: These results indicate that the prevalence of hypoalbuminemia is higher in individuals with motor disabilities than in healthy individuals and that inflammation is a strong negative correlate of serum albumin levels. Therefore, inflammation should be examined for the assessment of hypoalbuminemia among institutionalized individuals with motor disabilities.

• YAKHAK HOEJI
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• v.32 no.3
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• pp.182-186
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• 1988

Binding of four cephalosporins(cefaclor, cefpiramide, ceftazidime, ceforanide) to bovine serum albumin was studied. Difference spectrophotometry was employed to evaluate the nature and the degree of association of cephalosporin-albumin complex. 2-(4'-hydroxybenzen azo) benzoic acid was used as the uv spectrophotometric probe for measuring the binding of cephalosporins to bovine serum albumin. Competitive bindings between cephalosporins and probe were observed. For the binding of cephalosporins to bovine serum albumin, three binding sites were identified. The binding constants of cefaclor, ceforanide, ceftazidime and cefpiramide were $12.57\;{\times}\;10^{-2}M^{-1}$, $6.49\;{\times}\;10^{-2}M^{-1}$, $4.70\;{\times}\;10^{-2}M^{-1}$ and $6.20\;{\times}\;10^{-2}M^{-1}$ respectively.

• Clinics in Orthopedic Surgery
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• v.10 no.4
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• pp.398-406
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• 2018

Background: Hypoalbuminemia (serum albumin < 3.5 g/dL) is associated with increased morbidity and mortality in patients undergoing total hip arthroplasty (THA) and total knee arthroplasty (TKA). However, costs associated with hypoalbuminemia remain unknown. This study investigated the effect of serum albumin on direct treatment costs, length of stay (LOS), and readmissions for primary and revision THA and TKA patients. Methods: All adult patients at a single institution undergoing primary or revision THA or TKA between January 2014 and December 2016 were retrospectively reviewed. Patients were stratified by preoperative serum albumin level. The primary outcome was total direct costs at index hospitalization. Secondary outcomes included LOS and readmission within 30 days. Multivariable regressions were utilized to adjust for demographics and comorbidities. Results: Of 3,785 patients, 114 (3.0%) had hypoalbuminemia. After adjustment, hypoalbuminemia was associated with a 16.2% increase in costs (${\beta}=0.162$; 95% confidence interval [CI], 0.112 to 0.213; p < 0.001), representing an average cost increase of $3,383 (95% CI, $2,281 to $4,485) relative to costs for serum albumin > 4.5 g/dL. The increased total costs were significantly higher in revision ($4,322, p = 0.034) than in primary ($3,446, p < 0.001) procedures. In adjusted regression, each 1.0 g/dL increase in serum albumin yielded a 6.6% reduction in costs (${\beta}=-0.066$; 95% CI, -0.090 to -0.042]; p < 0.001), for average savings of $1,282 (95% CI, $759 to $1,806) per unit albumin. Adjusted regressions demonstrated that a 1-point increase in serum albumin reduced readmissions by 53% (odds ratio, 0.47; 95% CI, 0.31-0.73; p = 0.001) and LOS by 0.6 days (${\beta}=-0.60$; 95% CI, -0.76 to -0.44; p < 0.001). Conclusions: Hypoalbuminemia is associated with increased total direct costs, LOS, and readmissions following primary and revision THA and TKA. Future efforts to predict and address total costs should take into consideration the patient's preoperative serum albumin levels.

• Korean Journal of Agricultural Science
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• v.14 no.2
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• pp.413-421
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• 1987

The objective of this study was to evaluate the possibility of sex preselection by gradients methods using bovine serum albumin in rabbits. Artificial insemination with separated sperm was performed, after highly motile sperm were separated by different methods using 6%, 10% and 20% bovine serum albumin. Various characteristics of separated sperm, and the conception rate and secondary sex ratio at artificial insemination with sperm separated by different methods were compared. The results obtained were as follows. 1. The conception rate of sperm separated by bovine serum albumin gradients was higher than th at of control sperm. But secondary sex ratio was not altered by this methods. 2. The sperm separated by bovine serum albumin gradients showed significantly high value in motility, percent of normal sperm and progressive motility as compared with control sperm and revealed the highest sperm recovery when separated with 6% bovine serum albumin. 3. The sperm motility, percent of normal sperm and progressive motility of the highly motile sperm frozen after being separated from raw semen with bovine serum albumin, showed significantly high value than those of control sperm.

• Archives of Pharmacal Research
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• v.6 no.1
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• pp.63-68
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• 1983

The binding properties of three ginsenosides, Rb$_{1}$, Rc and Re, to bovine and human serum albumins have been examined by fluorescence probe technique. 1-anilinonphathalene-8-sulfonate (ANS) was used as the fluorescence probe. Protopanaxatriol glycoside, Re, did not quench the fluorscence of ANS to the bovine serum albumin. Competitive bindings between protopanaxadiol glycosides, Rb$_{1}$ and Rc are both 3.3 . The binding constants for Rb$_{1}$ and Rc with bovine serum albumin were 1.91 * 10$_{4}$M$_{-1}$ AND 1.04 * 10$^{[-994]}$ M$^{-1}$ , respectively. The ginsenosides, Rb$_{1}$, Rc and Re did not quench the fluorescence of ANS bound to human serum albumin.