• Korean Journal of Veterinary Research
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• v.15 no.1
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• pp.19-22
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• 1975

The serum albumin phenotypes and the gene frquencies of 100 Korean native goats were examined by starch gel electrohporesis. The results obtained were as follows: 1. The albumin phenotypes were classified as Alb AA, Alb AB, and Alb BB and the frequencies of appearence were 10, 12 and 78%, respectively. 2. The genetic factors of serum albumin were observed as Alb A and Alb B and the rates of gene frequencies were 16 and 84%, respectively.

• Archives of Pharmacal Research
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• v.9 no.2
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• pp.87-91
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• 1986

In attempt to develop a drug delivery system using serum albumin microspheres, bovine serum albumin microspheres containing antitumar agent. Cytarabine, were prepared. The shape, surface characteristics, size distribution, behavior of in vivo distribution, drug release behavior, and degradation of albumin microsphers in animal liver issue homogenate and proteolytic enzyme were investigated. The shape of albumin microspheres was spherical and the surface was smooth and compact. The size distribution of the albumin microspheres was effected by dispertion forces during emulsification and albumin concentration. Distribution of albumin microspheres after imtravenous administration in rabbit was achieved immediately. In vitro, albumin microsphere matrix was so hard that it retained most of cytarabine except initial burst during the first 10 minutes, and the level of drug release during the initial burst was affected by heating temperature, drug/albumin microsphere matrix was so hard that it retained most of cytarabine except initial burst during the first 10 minutes, and the level of drug release during the initial burst was affected by heating temperature, drug/albumin concentration ratio and size distribution. After drug release test, the morphology of albumin microspheres was not changed. Albumin microsphere matrix was degraded by the animal liver issue homogenate and proteolytic enzyme. The degree of degradation was affected by heating temperature.

• Korean Journal of Veterinary Research
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• v.24 no.2
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• pp.245-266
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• 1984

As a fundamental study to increase the reproductive efficiency in cattle, highly motile sperm were separated and collected from raw semen, extended semen and frozen semen by different methods using various concentrations of bovine serum albumin or Tyrode's solution. Various characteristics and light microscopic and electron-microscopic morphology of sperm separated by different methods were compared. The results obtained were as follows; 1. The sperm separated from raw semen using bovine serum albumin showed significantly high value in motility, motile sperm count, percent of normal sperm and progressive motility, as compared with control sperm and revealed the highest sperm recovery rate when separated with 6% bovine serum albumin. 2. 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 a control sperm and especially found the highest value when separated with 20% bovine serum albumin. 3. Light-microscopic percent of abnormality was significantly low in the prefrozen and postfrozen highly motile sperm separated with bovine serum albumin, as compared with control sperm. 4. Electron-microscopic finding of the highly motile sperm separated with bovine serum albumin showed low percent of deformity in the dilatation and vesiculation of cell membrane, in dilatation and density loss of acrosome than in those of control sperm. 5. It was impossible to separate the highly motile sperm from frozen semen with bovine serum albumin, but it was possible with Tyrode's solution. 6. Recovery rate of highly motile sperm from raw semen extended semen and frozen semen was the highest when the sperm pellet stood in Tyrde's solution for 80 minutes. 7. The highly motile sperm separated from raw semen, extended semen and frozen semen with Tyrode's solution showed significantly high value in motility, progressive motility and percent of normal sperm, as compared with control sperm. 8. Highly motile sperm, when separated from raw semen, extended semen and frozen semen with Tyrode's solution, showed significantly low percent of microscopic abnormality as compared with control sperm.

• Archives of Pharmacal Research
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• v.8 no.3
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• pp.159-168
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• 1985

In attempt to develop a drug delivery system using serum albumin microspheres, bovine serum albumin microspheres containing antitumor agent, cytarabine, were prepared. The shape, surface characteristics, size distribution, behavior of in vitro distribution, drug release behaior, and degradation of albumin microspheres in animal liver tissue homogenate and proteolytic enzyme were investigated. The shape of albumin microspheres was spherical and the surface was smooth and compact. The size distribution of the albumin microspheres was affected by dispersion forces during emulsification and albumin concentration. Distribution of albumin mirospheres after intravenous administration in rabbit was achieved immediately. In vitro, albumin microsphere matrix was so hard that it retained most of cytarabine except initial burst during the first 10 minutes, and the level of drug release during the initial burst was affected by heating temperature, drug/albumin concentration ratio and size distribution. After drug release test, the morphology of albumin micropheres was not changed. Albumin microsphere matrix was degraded by the rabbit liver tissue homogenate and proteolytic enzyme. The degree of degradation was affected by heating temperature.

• Bulletin of the Korean Chemical Society
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• v.35 no.7
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• pp.2114-2122
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• 2014

The association of silybin with ${\beta}$-cyclodextrin and its influence on silybin's binding with bovine serum albumin are reported. The stoichiometry, binding constant, and the structure of silybin-${\beta}$-cyclodextrin inclusion complex are reported. The titrations of silybin with bovine serum albumin in the absence and presence of ${\beta}$-cyclodextrin are carried out and the differences in binding strengths are discussed. Molecular modeling is used to optimize the sites and mode of binding of silybin with bovine serum albumin. F$\ddot{o}$rster resonance energy transfer is calculated and the proximity of interacting molecules is reported in the presence and absence of ${\beta}$-cyclodextrin.

• Journal of Pharmaceutical Investigation
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• v.19 no.1
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• pp.15-20
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• 1989

The displacement of protein bound sulfonamides (sulfisoxazole, sulfamethoxazole, sulfisomidine) by furosemide was investigated in bovine serum albumin by equilibrium dialysis method. Furosemide $(2{\times}10^{-4}M)$ in bovine serum albumin ($7.24{\times}10^{-5}$, $1.45{\times}10^{-4}$, $2.89{\times}10^{-4}M$). Sulfisoxa캐1e and furosemide were bound reversibly to bovine serum albumin and competitive for the same binding sites when administered together. Consequently, dosage regimen of sulfisoxazole should be adjusted carefully when sulfisoxazole is administered along with furosemide.

• Archives of Pharmacal Research
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• v.12 no.3
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• pp.160-165
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• 1989

Binding of sulfaethidole to bovine serum albumin was studied by equilibrium dialysis, fluorescence probe technique, uv difference spectrophotometry and circular dichroism. Equilibrium dialysis method enabled us to estimate the total number of drug binding sites of albumin molecule. For sulfaethidole, albumin had 6 primary and 40 secondary binding sites. The primary and secondary binding constants were 0.9 * 10/sup 5/ M/sup -1/ and 0.2 * 10/sup 6/ M/sup -1/, respectivitely. 1-Anilino-8-naphthalenesulfonate (ANS) and 2-(4-hydroxylbenzeneazo)- benzoic acid (HBAB) were used as the fluorescence probe and the uv spectrophotometric probe, respectively. In fluorescence probe technique, results indicated that the number of higher affinity drug binding site of albumin was 1 and the number of lower affinity drug binding sites of albumin was 3, and the primary and secondary drug binding constants for bovine serum albumin were 2.15 * 10/sup 5/M/sup -1/ and 1.04 * 10/sup 5/ M/sup -1/, respectively. In uv difference spectrophotometry, binding sites were 3 and binding constant was 1.88 * 10/sup 5/M/sup -1/. The above spectrophotometry, binding sites were 3 and binding constant was 1.88 * 10/sup 5/M/sup -1/. The above results suggest that several different methods should be used in ompensation for insufficient information about drug binding to albumin molecule given by only one method.

• Journal of Nutrition and Health
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• v.46 no.6
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• pp.521-530
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• 2013

Protein-energy malnutrition, PEM, and increased hs-CRP level are considered to be associated with increased risk of cardiovascular disease (CVD) in hemodialysis (HD) patients. This is commonly referred to as the vicious circle of malnutrition-inflammation-atherosclerosis cardiovascular disease (MIA syndrome) in chronic kidney disease (CKD). Low protein intake can decrease the serum level of albumin and increase inflammational markers; further, both low serum albumin and high hs-CRP are independent risk factors for all-cause mortality in HD patients. The aim of this study is comparing the serum levels of albumin and hs-CRP in HD patients according to the protein intake levels. The total number of subjects was 60 hemodialysis patients; they were grouped by dietary protein intake: low protein intake group (LPI, protein intake < 1.0 g/kg IBW, 11 men and 19 women) and adequate protein intake group (API, protein intake ${\geq}$ 1.0g/kg IBW, 12 men and 18 women). Blood biochemical parameters, nutrient intake, and dietary behaviors were compared between the LPI and API groups. The LPI group showed a significantly lower serum level of albumin and higher serum level of hs-CRP than the API group (p < 0.05). The LPI group showed a significantly lower intake of most nutrients than the API group (p < 0.05). Index of Nutritional Quality of most nutrients of the LPI and API groups were lower than 1.0. Dietary protein intake was positively correlated with the serum level of albumin (r = 0.306, p < 0.05) and negatively correlated with the serum level of hs-CRP (r = -0.435, p < 0.01). The serum level of hs-CRP was negatively correlated with that of albumin (r = -0.393, p < 0.01). According to these result, serum albumin and hs-CRP in HD patients were influenced by the protein intake levels. To prevent MIA syndrome, it is necessary to improve nutritional status, especially in protein and energy.

• Toxicological Research
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• v.16 no.3
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• pp.221-227
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• 2000

A 6-sulfooxymethylbenzo[a]pyrene (SMBP), the ultimate metabolite of methyl-substituted benzo[a]pyrene (BP), has been found to be carcinogenic in mice. These properties may be attributable to its strong reactivity with cellular macromolecules such as DNA. However, serum and its major constituent albumin attenuated significantly the cytotoxicity and mutagenicity of 5MBP in bacterial and mammalian cell systems. This inhibitory activity of serum against 5MBP-induced cytotoxicity and mutagenicity in Chinese hamster V79 cells appears to be caused by the reduced macromolecular adducts such as DNA and proteins, but serum failed to reduce 5MBP binding to naked calf thymus DNA. A number of proteins in the serum could act as nucleophiles that are able to intercept reactive chemicals through covalent binding. Albumin present in the plasma seems to be one of major components responsible for direct binding with 5MBp, thereby reducing its reactivity to genetic materials. We here determined which fraction is preferential for 5MBP binding through fractionation of 5MBP-treated serum with ammonium sulfate. The albumin-containing fraction had slightly more affinity for 5MBP than the immunoglobulin-containing fraction. Our results indicate that the covalent modification of plasma proteins may reduce 5MBP-induced damage.

• Archives of Pharmacal Research
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• v.7 no.1
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• pp.11-15
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• 1984

Binding of sic cephalosporins (cefotaxime, cefuroxime, cafazoline, cephalothin, cephaloridine, cephacetrile) to human serum albumin was studied. Fluorescence probe technique and difference spectrophotometry were employed to evaluate the nature and degree of association of cephalosporin-albumin complex. 1-anilinonaphthalene-8-surfonate was used as the fluorescence probe, and 2-(4'-hydroxybenzeneazo)benzoic acid as the UV spectrophotometric probe. Competitive bindings between cephalosporins and probe were observed. For the binding of cephalosporins to human serum albumin, three binding sites were identified by fluorescence probe technique but four binding constants of cephalosporins to human serum albumin measured by fluorescence probe technique are higher than those meausred by UV spectrophotometry.