• Journal of Photoscience
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• 제12권1호
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• pp.25-32
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• 2005

Binding of N-Alkyl phenothiazines (NAP) to bovine serum albumin (BSA) was studied by spectroscopic methods.It was found that the phenothiazine ring common to all drugs makes major contribution to interaction. However, the nature of alkylamino group at position 10 influences the protein binding significantly. Stern-Volmer plots indicated the presence of static component in the quenching mechanism. The high magnitude of rate constant of quenching indicated that the process of energy transfer occurs by intermolecular interaction and thus the drug-binding site is in close proximity to tryptophan residues of BSA. Binding studies in presence of hydrophobic probe, 8-anilino-1-naphthalein-sulphonic acid showed that there is hydrophobic interaction between drug and the probe and they do not share common sites in BSA. Thermodynamic parameters obtained from data at different temperatures showed that the binding of NAP to BSA predominantly involve hydrophobic forces. The effects of some cations and anions common ions were investigated on NAP-BSA interactions. The CD spectrum of BSA in presence of drug showedthat binding of drug leads to change in the helicity of the protein.

• 대한한방내과학회지
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• 제29권1호
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• pp.104-116
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• 2008

Objective : Membranous nephropathy (MN) is the most common cause of adult nephrotic syndrome worldwide. MN has been defined as granular subepithelial deposition of IgG immune complexes along the glomerular basement membrane (GBM). We aimed to identify the effects of Chungyeolmaksungbang (CYMSB) treatment on cBSA-induced in MN mouse model. Methods : The effect of Chungyeolmaksungbang treatment was studied on the morphology and protein excretion in the cationized bovine serum albumin (cBSA)induced mouse chronic serum sickness nephritis model. One group of mice was given intra-peritoneal (i.p.) immunizing doses of cBSA and complete Freund's adjuvant. One week later, these animals began a single i.p. injection of cBSA for 4 weeks. A second group followed the same injection protocol, but was given CYMSB p.o. Results : Proteinuria significantly was decreased and serum albumin was increased in the group treated with cBSA and CYMSB extract compared with the control. Serum BUN was significantly decreased on CYMSB compared with control. CD3e+/CD19 cells ratio of peripheral blood was decreased and CD4+/CD8 cells was increased. Level of $IL-1{\beta}$ was significantly decreased, and $IFN-{\gamma}$ was significantly increased. Concentration of IgG and IgM was significantly decreased compared with control. Thickness of GBM was decreased on histological analysis of kidney. Deposition of CD4 and CD8 was decreased on immunohistochemical staining of kidney. Conclusions : We conclude that CYMSB treatment may could be a useful remedy agents for treating the MN with cBSA.

• 대한화학회지
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• 제36권2호
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• pp.329-334
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• 1992

단백질 수용액 중의 초음파흡수 mechanism을 규명하기 위하여 pH 7의 소혈청 albumin(BSA)수용액의 초음파흡수 측정을 주파수 100 kHz에서 1600 MHz에 걸쳐 행하였다. 측정방법은 plano-concave 공명법(0.1${\sim}$10 MHz)과 고분해능 Bragg 반사법(120${\sim}$1600 MHz)을 사용하였다. pH7에서의 초음파흡수스펙트럼은 Davidson-Cole 분포식의 거울상인 분포함수를 사용한 완화곡선과 일치하였다. 이 완화현상을 BSA 분자의 수화평행에 의한 것으로 해석하였다.

• Journal of Photoscience
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• 제11권2호
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• pp.65-69
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• 2004

The mechanism of interaction of four coumarin derivatives (CDS) with bovine serum albumin (BSA) was studied using spectrofluorometric technique. It was found that the coumarin ring common to all CDS makes major contribution to interaction. Binding affinities could be related to parachor values of CDS. Stem-Volmer plots indicated the presence of static component in the quenching mechanism. Results also showed that both tryptophan residues of protein are accessible to CDS. The high magnitude of rate constant of quenching indicated that the process of energy transfer occurs by intermolecular interaction forces and thus CDS binding site is in close proximity to tryptophan residues of BSA. Binding studies in the presence of the hydrophobic probe, 8-anilino-l-naphthalein-sulfonic acid showed that there is hydrophobic interaction between CDS and the probe and they do not share common sites in BSA. Thermodynamic parameters obtained from data at different temperatures showed that the binding of CDS to BSA involve hydrophobic bonds predominantly. The effects of various metal ions on the binding of CDS with BSA were also investigated.

• Journal of Photoscience
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• 제12권3호
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• pp.113-117
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• 2005

Spectroscopic investigations on the interaction of gabapentin (GBP) with bovine serum albumin (BSA) were reported. The association constant of GBP-BSA system was determined at different temperatures (298, 302, 306 and 311 K) based on the fluorescence quenching results. The GBP was found to quench the fluorescence of BSA through static mechanism. Thermodynamic parameters, the standard enthalpy change, $({\Delta}H^o)$ and the standard entropy change $({\Delta}S^o)$ were observed to be $-9.61{\pm}0.008\;kJ\;mol^{-1}$ and $3.58{\pm}0.011\;Jmol^{-1}K{-1}$ respectively. These indicated that the hydrophobic and electrostatic forces played a role in the interaction of GBP with BSA. The negative value of ${\Delta}G^o$ revealed that the binding reaction is spontaneous. The circular dichroism studies indicated the conformational changes in BSA upon interaction with GBP. The effect of some metal ions on the binding constant was also investigated.

• Bulletin of the Korean Chemical Society
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• 제24권1호
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• pp.45-48
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• 2003

A novel fluorimetric method has been developed for the determination of microgram quantities of bovine serum albumin (BSA) based on its enhancement effect of Nile Blue fluorescence at 670 nm, caused by binding of Nile Blue to BSA to produce a stable water soluble complex. The binding constant of micromole Nile Blue-BSA complex was estimated by Scatchard plot method. Under the optimal conditions, the increased fluorescence intensity was linearly related to BSA concentration in the range of 0.5-12.0 ㎍/mL. The detection limit was 0.2 ㎍/mL, and the relative standard deviation of six replicate measurements was 1.4% for 10.0 ㎍/mL BSA. There was little interference from amino acids, sugars and most of metal ions.

• 한국가금학회지
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• 제26권4호
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• pp.247-252
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• 1999

This experiment was carried out to investigate the effects of the laying hens on the immune response against bovine serum albumin(BSA) in egg yolk. Total 45 laying hens were divided into three groups according to breeds (White Leghorn, ISA Brown, Native hen). They were fed the experimental diet for 12 weeks. Immune response were examind in egg yolk from three groups of hens injected with BSA. The results obtained from this work were summaried as follows : 1. The weight of egg yolk and the percentage of hen-day production in the ISA Brown hens are greater than those in the Native hens and the White Leghons. 2. IgY concentrations in eggs from hens immunized with BSA were not different among the breeds laying hens. 3. The anti-BSA antibody activities determined by enzyme linked immunosorbent assay (ELISA) in the egg yolk were similar between the White-Leghorn and ISA Brown hens, but Native hens tended to decrease in 20∼50 days respectively. Therefore, the weight of egg yolk and the percentage of hen-day production in the ISA Brown hens are greater than those in the Native hens and the White Leghons will be as important factors for an efficient production of IgY.

• 대한한의학회지
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• 제30권4호
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• pp.93-107
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• 2009

Objective: Membranous nephropathy (MN) is one of the most common causes of nephrotic syndrome in adults. However, there is not a satisfactory treatment for MN. This study aimed to evaluate the effect of Houttuyniae Herba Extract (HHE) on MN induced by cationic bovine serum albumin (cBSA). Methods: Mice were divided into 4 groups. The first group, Normal, was injected with saline. The second group, Control, was treated with cBSA (10mg/kg i.p) only. The third group, HHE-250, was treated with cBSA (10mg/kg i.p) and HHE (250mg/kg, p.o). The fourth group, HHE-500, was treated with cBSA (10mg/kg i.p) and HHE (500mg/kg, p.o). After treatment for 4 weeks, we measured change of body weight, 24 hrs proteinuria, serum albumin, total cholesterol, triglyceride, BUN, creatinine, IgA, IgM, IgG, TNF-${\alpha}$, IL-1${\beta}$ levels and the mRNA expression of IFN-${\gamma}$, IL-6, and IL-10. The morphologic changes of renal glomeruli were also observed with a light microscope and an electron microscope. Results: The levels of 24 hrs proteinuria and serum triglyceride, BUN, IgG, TNF-${\alpha}$, IL-1${\beta}$ significantly decreased in both HHE groups, while the level of serum albumin significantly increased in both HHE groups. The mRNA expression of IFN-${\gamma}$ and IL-6 in splenocytes considerably increased in both HHE groups. The mRNA expression of IL-10 in splenocytes considerably decreased in both HHE groups. In histological findings of kidney tissue, thickening of GBM decreased in both HHE groups. Conclusions: This study shows that HHE might be effective for treatment of acute stage MN. More clinical data and studies are to be done for efficient application.

• 센서학회지
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• 제30권5호
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• pp.326-330
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• 2021

Reactions between gold (Au) surface plasmon resonance (SPR) chips and bovine serum albumin (BSA) dissolved in solutions of different pH were investigated. The charge on the BSA depends on the pH of the solution in which it is dissolved. Thus, dissolving BSA in different pH solutions resulted in different charges of BSA. Among the BSA dissolved in solutions with pH 4.01, 7.4, and 10.01, the SPR response was the highest for BSA dissolved in the solution of pH 4.01. To eliminate the response variation owing to the difference in the refractive indices of the solutions, phosphate buffered saline (PBS) was injected into the system after the reaction of BSA with the Au SPR chip had happened. In this case too, the BSA dissolved in the solution with pH 4.01 exhibited the highest response. This may be attributed to the non-uniform distribution of ionic patches on the BSA, which can induce electrostatic attraction to the surface even though BSA has a positive charge at pH 4.01, and the absolute values of the net charge of BSA at pH 4.01 and 7.4 were very close.

• Journal of Photoscience
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• 제11권1호
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• pp.29-33
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• 2004

The mechanism of interaction of cyanocobalamin (CB) with bovine serum albumin (BSA) has been investigated by spectrofluorometric and circular dichroism methods. Association constant for the CB-BSA system showed that the interaction is non-covalent in nature. Binding studies in the presence of an hydrophobic probe, 8-anilino-l-naphthalene sulphonic acid, sodium salt (ANS) showed that there is hydrophobic interaction between CB and ANS and they do not share common sites in BSA. Stern-Volmer analysis of fluorescence quenching data showed that the fraction of fluorophore (protein) accessible to the quencher (CB) was close to unity indicating thereby that both tryptophan residues of BSA are involved in drug-protein interaction. The rate constant for quenching, greater than $10^{10}$ $M^{-1}$ $s^{-1}$, indicated that the drug binding site is in close proximity to tryptophan residue of BSA. Thermodynamic parameters obtained from data at different temperatures showed that the binding of CB to BSA involves hydrophobic bonds predominantly. Significant increase in concentration of free drug was observed for CB in presence of paracetamol. Circular dichroism studies revealed the change in helicity of BSA due to binding of CB to BSA.