• Journal of Biomedical Engineering Research
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• v.14 no.3
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• pp.209-220
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• 1993

Microspheres are expected to be applied to biomedical areas such as solid-phase immunoassays, drug delivery systems, Immunomagnetic cell separation. To synthesize micro-spheres for biomedical application, "two stage shot growth method" was developed. The uniformity ratio or synthesized microspheres was always smatter than 1.05. And the surface charge density (or the number of ionizable functional groups) of the microspheres synthesized by "two stage shot growth method" was 6-13 times higher than thats of the ml crospheres synthesized by conventional seeded batch copolymerization. As a previous step for biomedical application, adsorption experiments of bovine albumin on microspheres were carried out under various conditions. The maximum adsorbed amount was obtained in the neighborhood of pH 4.5. Isoelectric point of bovine albumin Is pH 5.0, so experimental result shows that it shifted to acid area. The adsorption Isotherm was obtained, the plateau region was always reached at 2.Og/L (bulk concentration of bovine albumin ) . The effect of the kind and the amount of surface functional group was also examined.p was also examined.

• 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.

• Korean Journal of Veterinary Research
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• v.29 no.1
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• pp.57-60
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• 1989

This study was carried out to evaluate the possibility of sex preselection by gradients methods using bovine serum albumin in rabbits. Artificial insemination was performed with sperm from the top and bottom layer of rabbit semen separated by bovine serum albumin gradients. Various characteristics of separated sperm, and the conception rate and secondary sex ratio at artificial insemination with separated sperm were compared. The results obtained were as follows. 1. The sperm from the bottom layer showed significanty high value in motility, percent of normal sperm and progressive motility as compared with control sperm and the sperm and the sperm from the top layer. 2. The conception rate of sperm from the bottom layer was higher than that of the top layer. But secondary sex ratio was not altered by this methods.

• 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.

• Microbiology and Biotechnology Letters
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• v.29 no.4
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• pp.248-252
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• 2001

Recombinant Human serum albumin (rHSA) was purified to near homogeneity from H, polymorpha using heat treatment, ultrafiltratipn and Phenyl Sepharose CL-4B and Mono Q column chro - matographies with a recovery yield of 60% The molecular weight of the purified rHSA was estimated to be about 65,000 Da by denaturing SDS-PAGE The N terminal amino acid sequence of the purified HSA determined by Edman degradation was turned out to be Asp- Ala- His- Lys- Ser- Glu- Ala, suggesting that the rHSA expressed in H, polymorpha was efficiently secreted and correctly processed at the cleavage site of secretion signal sequence. The purified human albumin showed the pI value identical to that of authentic human serum albumin.

• Journal of Pharmaceutical Investigation
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• v.25 no.2
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• pp.101-108
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• 1995

The surface of albumin microspheres could be modified with methotrexate (MTX) by using 1,3-dicyclohexylcarbodiimide (DCC). Surface-modified albumin microspheres entrapping no MTX (SAMS), free MTX (SAMSF) and MTX-bovine serum albumin (BSA) conjugates (SAMSC) were prepared. respectively, and their release characteristics were investigated in the presence of trypsin using a dissolution tester. The mean diameters of all the microspheres were $5{\sim}8\;{\mu}m$, and their shapes was small and uniform. MTX bound tn their surfaces was released slower than the entrapped free MTX, and laster than the entrapped MTX-BSA conjugates. Also, surface-modified MTX was scarcely released in the absence of a proteolytic enzyme. Therefore, the surface-modified MTX may be released rapidly from SAMSC at the target site, and thereafter MTX may be released slowly from the encapsulated MTX-BSA conjugates in SAMSC for a long period.

• Asian-Australasian Journal of Animal Sciences
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• v.15 no.11
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• pp.1559-1563
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• 2002

The ovarian follicular fluid was found to contain steroidogenesis stimulatory protein similar to albumin from human and buffalo. Therefore, the albumins from various species, commercial and purified, were studied for their steroidogenic effect on progesterone secretion by granulosa cells from buffalo ovaries, during culture. A dose of $20{\mu}g$ of bovine serum albumin was optimum to exhibit maximum progesterone secretion on day 6 of culture, in medium ($350{\mu}l$) containing $10^5$ cells. Among commercial albumins, chicken albumin showed highest effect on progesterone secretion, which was followed by albumins from goat, bovine, human, sheep and rat, respectively at day 6 of culture. The albumins were also purified from blood serum of buffalo, goat and rat using salt fractionation, ion-exchange chromatography, gel filtration and SDS-PAGE. The highest stimulatory effect on progesterone secretion was shown by albumin purified from buffalo blood serum and lowest by that from rat blood. Comparatively the buffalo and goat albumins were more biologically active than commercial albumins. The presence of some active molecules conjugated with freshly purified albumins may be responsible for better stimulatory effect.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.34 no.5
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• pp.473-477
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• 2001

Chitosan has been used as an effective adsorbant for the treatment of wastewater from seafood processing. We investigated the effects of deacetylation degree (DD) and molecular weight (MW) of chitosan on protein adsorption ability and also the optimum conditions of chitosan treatment for protein adsorption in 3 kinds of protein (albumin, hemoglobin and albumin-myoglobin mixture) solutions. The higher deacetylation degree and the lower molecular weight chitosan, the higher adsorption for water soluble proteins was accomplished. The optimum pHs for adsorption of albumin, hemoglobin and albumin-myoglobin mixture (4: 1, w/w) were 4.0, 7.0 and 4.0 respectively and the optimum time was $3\~4$ hrs for all proteins. Sodium chloride in the model system of protein solution was a preventing factor for protein adsorption ability of chitosan (DD=$80\%$, MW=350 kDa).

• 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.