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

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

• 대한화학회지
• /
• 제36권2호
• /
• pp.329-334
• /
• 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
• /
• 제11권2호
• /
• pp.65-69
• /
• 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.

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

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

• Journal of Photoscience
• /
• 제12권1호
• /
• pp.11-15
• /
• 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

• 미생물학회지
• /
• 제25권4호
• /
• pp.274-281
• /
• 1987

Candida pseudotropicalis의 영양요구성 돌연변이 균주들에 대한 원형질체 형성, 재생 그리고 융합에 있어서 bovine serum albumin (BSA), myoinositol 그리고 ergosterol의 증진효과를 연구하였다. 원형질체 형성율은 영양요구성 균주의 type에 따라 48%-98%였다. O. 5mg/ml의 myoinositol과 0.1mg/ml의 ergosterol을 배양액에 첨가하고 4mg/ ml의 BSA을 원형 질체 형성 완충용액에 첨가했을 때는 50~100%의 원형절체 형성윷을 얻었다. 영양요구성 균주의 생장배지에 myoinositol과 ergosterol을 동시에 첨가하고 원형질체 형성 완충용액에 BSA를 침가하면 2.2-3.0애의 원형질체 재생율 증진을 보여주었다. 원형질체 융합의 최적조건에서 상보적 영양요구성 균주간의 융합율은 $7.0\times 10^{-4}$ ~ $1.5\times 10^{-3}$ 이였으며 상기화합물을 처리하지 않고 얻은 융힐l율과 비교해서 1. 9-2. 3배의 증가를 보였다. 이러힌 결과로 본 연구에서 사용된 균주들에서는 상기화합물 처리 에 의해 원형질체 재생은 물론 세포융합율도 증진됨을 알 수 있었다.

• Membrane and Water Treatment
• /
• 제2권2호
• /
• pp.91-103
• /
• 2011

The flux behavior in the separation of equimolar bovine serum albumin (BSA) and bovine hemoglobin (HB) in aqueous solutions by cross-flow ultrafiltration (UF) was investigated, in which polyacylonitrile membrane with a molecular weight cut-off (MWCO) of 100 kDa was used. BSA and HB have comparable molar mass (67,000 vs. 68,000) but different isoelectric points (4.7 vs. 7.1). The effects of process variables including solution pH (6.5, 7.1, and 7.5), total protein concentration (1.48 and 7.40 ${\mu}M$), transmembrane pressure (69, 207, and 345 kPa), and solution ionic strength (with or without 0.01 M NaCl) on the separation were examined. It was shown that the ionic strength had a negligible effect on separation performance under the conditions studied. Although BSA and HB are not rigid bodies, the flux decline in the present cross-flow UF did not result from the mechanism of cake filtration with compression. In this regard, the specific cake resistance when pseudo steady-state was reached was evaluated and discussed.

• Archives of Pharmacal Research
• /
• 제14권4호
• /
• pp.336-341
• /
• 1991

The effect of bovine serum albumin (BSA) on the encapsulation efficiency and stability of liposomes containing methotrexate (MTX) having different surface charges and cholesterol contents were investigated. The encapsulation efficiency of MTX was lower and the release of MTX was faster by the addition of BSA. The leaking of MTX from lipid bilayer depends upon the BSA concentrations. These results may be derived from the interaction of BSA with lipid bilayers. The dynamic structural changes of BSA were monitored indirectly using circular dichroism spectra. Observed dynamic structural changes of BSA with liposomes are presumed to reflect the interaction of BSA with liposomes. Negatively charged liposomes have more strong interaction with BSA than neutral and positively charged liposomes. BSA attacks lipid bilayers whether it is at the inner or at the outer phase of lipid bilayer and induces leakage of entrapped MTX. Especially, negatively charged liposomes are more sensitive than others. The inclusion of cholesterol in the lipid layers inhibits the interaction of BSA with liposomes and shows protective effect against BSA-induced leakage of MTX. To endure the attacking of BSA liposomes as drug carriers should be made using cholesterol.