• 제목/요약/키워드: BSA (Albumin, from bovine serum)

검색결과 152건 처리시간 0.029초

메토트렉세이트가 표면수식된 알부민 미립구의 제조 및 특성 (Preparation and Characteristics of Surface-Modified Albumin Microspheres with Methotrexate)

  • 황성주;조항범;이계주;김종국
    • Journal of Pharmaceutical Investigation
    • /
    • 제25권2호
    • /
    • pp.101-108
    • /
    • 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.

  • PDF

Studies on the interaction of edible dyes with protein I

  • Jang, Seong-Ki;Kim, Bak-Kwang;Lee, Wang-Kyu
    • Archives of Pharmacal Research
    • /
    • 제8권3호
    • /
    • pp.169-175
    • /
    • 1985
  • The binding of bovine serum albumin (BSA)-edible dyes was studied by spectrophotometric method. The edible dyes used in this study were amaranth, erythrosine, tartrazine and sunset yellow. The binding free energies and binding sites were determined at pH 7.4. The ranges of edible dye concentration were from 0.3 to $7{\times}10^{-5}$M, and those of BSA were from 0.15 to $3{\times}10^{-5}$M. The binding free energies of BSA-edible dyes were from -6, 300 to -8, 100 cal/mole.

  • PDF

정자의 수정능력획득 과정 동안 정자표면의 Albumin의 이탈현상 (Loss of Surface-Associated Albumin during Capacitation and Acrosome Reaction of Mouse Epididymal Sperm in vitro)

  • 계명찬;김문규
    • 한국동물학회지
    • /
    • 제38권4호
    • /
    • pp.514-522
    • /
    • 1995
  • 생쥐 정자의 수정능력 획득과정 및 첨체반응을 전후로 정자표면과 albumin의 상호작용을 조사하였다. 부정소 정자를 체외에서 배양하는 과정에서 정자표면에서 이탈된 단백질의 분석과 함께 FITC-bovine serum albumin으로 정자를 형광염색하여 정자표면에 대한 albumin의 결합양상의 변화를 조사하였다. 90분간 정자를 배양한 수 정자를 제거한 후 농축한 배양액내에 정자 또는 부정소액에서 기원한 여러종의 단백질가 함께 albumin이 다량으로 발견되었다 정자의 체외배양 과정에서 일어나는 albumin의 이탈은 배양액내의 $Ca^2$+과 무관하게 일어났다. BSA-FITC는 정소내 정자의 두부표면에 미약하게 결합한 반면 미부부정소 정자의 첨체표면에는 다량 결합하였다. $Ca^2$+-ionophore인 A23187으로 첨체반응을 유발한 정자의 두부 표면에서는 후첨체부위만이 강하게 염색되었다. 이러한 결과는 정소 및 웅성 생식수관니에서 정자표면에 부착된 albumin이 자성 생식수관을 거치는 동안 이탈됨을 시사하며 이러한 현상은 정자의 수정능력획득과 밀접한 관련이 있는 것으로 사료된다.

  • PDF

역삼투막 표면에 음이온 고분자 코팅을 통한 파울링 현상 감소연구 (Study on the Fouling Reduction of the RO Membrane by the Coating with an Anionic Polymer)

  • 조은혜;정성일;임지원
    • 멤브레인
    • /
    • 제22권6호
    • /
    • pp.481-488
    • /
    • 2012
  • 폴리아마이드 역삼투막 표면에 음이온 수용성 고분자인 poly(vinyl amine)(PVAm)을 코팅한 후 오염물질인 bovine serum albumin (BSA), humic acid (HA), sodium alginate (SA)에 대하여 파울링 개선효과가 있는지를 알아보고자 하였다. PVAm의 코팅과 파울링 여부는 scanning electron microscopy (SEM)을 통해 관찰하였다. BSA, HA, SA 100 ppm 공급원액을 이용하여 2, 4, 8 bar로 압력을 변화시켜 투과성능실험을 수행한 결과 PVAm으로 코팅되지 않은 막과 코팅된 막 모두 압력증가에 따라 파울링 현상이 심화되었으나 PVAm으로 코팅된 막이 BSA, HA, SA의 경우 모두에서 약 30%이상 투과도가 향상되어 파울링 개선효과가 나타나는 것을 확인할 수 있었다. HA > SA > BSA의 순으로 파울링 개선효과가 나타났으며 HA의 경우 가장 두드러지게 나타났다.

Preparation and Characterization of Bovine Serum Albumin-loaded Cationic Liposomes: Effect of Hydration Phase

  • Park, Se-Jin;Jeong, Ui-Hyeon;Lee, Ji-Woo;Park, Jeong-Sook
    • Journal of Pharmaceutical Investigation
    • /
    • 제40권6호
    • /
    • pp.353-356
    • /
    • 2010
  • Although liposomes have been applied as drug delivery systems in various fields, the usage was limited due to the low encapsulation efficiency compared to other carrier systems. Here, cationic liposomes were prepared by mixing 1,2-dioleoyl-3-trimethylammoniopropane (DOTAP) as a cationic lipid, 1,2-dioleoyl-sn-glycerol-phosphoethanolamine (DOPE) and cholesterol (CH), and the liposomes were hydrated by varying the aqueous phases such as phosphate-buffered saline (PBS), 5% dextrose, and 10% sucrose in order to improve the encapsulation efficiency of bovine serum albumin (BSA). The particle size and zeta potential were determined by dynamic light scattering method and in vitro release patterns were investigated by spectrophotometry. Particle size and zeta potential of liposomes were varied depending on the ratio of DOTAP/DOPE/CH in range of 270-350 nm and 0.8-9.7 mV, respectively. Moreover, the addition of polyethylene glycol (PEG) improved the encapsulation efficiency from 37% to 43% as well as reduced particle sizes of liposomes while the liposomes were hydrated in PBS. When the liposomes were hydrated with 10% sucrose, the encapsulation efficiency of BSA was higher than any other groups. Whereas PBS was used as hydration solution, lower encapsulation efficiency was obtained compared with other groups. More than 60% of BSA was released from the liposomes hydrated with 10% sucrose; thereafter another 20% of BSA was released. Therefore, release pattern of BSA from cationic liposomes was extended release in this study. From the results, cationic liposomes dispersed in 10% sucrose would be potential carrier with high encapsulation efficiency.

Fibrin glue로부터 Ampicillin-Na의 용출 및 Tissue adhesive로서의 접착력 (Release of Ampicillin-Na from fibrin glue and its adhesive strength as a tissue adhesive)

  • 유봉규;권익찬
    • 대한의용생체공학회:의공학회지
    • /
    • 제16권3호
    • /
    • pp.367-375
    • /
    • 1995
  • 광범위 항생물질인 Ampicillin sodium(AMP-Na)을 두가지 방법 즉, 단순섞임과 bovine serum albumin(BSA)으로 microsphere화한 후 loading 하는 방법으로 fibrin glue(FG)를 제조하였고 이 FG로부터 AMP-Na의 서방성 시험을 시도하였다. 단순섞임의 경우 fibrinogen(FBNG)의 농도를 조적함으로서 FG로부터 AMP-Na의 지속적 방출을 달성할 수 있었으며 특히 이 microsphere를 glutaraldehyde로 가교화시킴으로서 용출속도를 더욱 늦출 수 있었다.(tO.9 : 33hr). FG의 rat perironeum에 대한 접착력은 FBNG과 thrombin의 농도가 각각 5.0%, 25~50 NIHU/ml에서 최대로 나타났다. Factor XIII의 농도는 0~500 U/1g of FBNG의 범위내에서 접착력에 거의 영향을 미치지 않았으며 incubation time은 60분일 때 최대로 나타났다. FG에 AMP-Na 및 BSA micorsphere를 loading하여도 접착력에는 큰 영향을 미치지 않았다.

  • PDF

약물과 생체고분자 간의 상호작용(제 13보)-세파로친과 소혈청알부민의 결합에 미치는 이온강도, pH 및 온도의 영향 (Drug-Biomacromolecule Interaction (XIII)-Effect of ionic Strength, pH and Temperature on Binding of Cephalothin to Bovine Serum Albumin-)

  • 김종국;임연수;양지선;정은주
    • Journal of Pharmaceutical Investigation
    • /
    • 제19권3호
    • /
    • pp.163-171
    • /
    • 1989
  • To investigate the protein binding characteristics of cephalothin, the effects of ionic strength, pH and temperature on the binding of cephalothin to bovine serum albumin (BSA) were studied by UV difference spectrophotometric method. With increasing ionic strength at constant PH and temperature, association constant decreased, but the number of binding sites sites was about 2 constantly. It may be deduced that the binding process is not only due to electrostatic forces. And the increased association constant at high ionic strength is explained by conformational changes of BSA from complex to subunits. The pH effect on the affinity of interaction indicated that the binding affinity of drug is higher in the neutral region than in the alkaline region. And, at high pH value, the number of binding sites decreased from 2 to 1 because of the conformational changes of BSA in alkaline region. The decrease in binding affinity of BSA to drug with increasing temperature was characteristic of an exothermic reaction. And the negative sign of ${\Delta}G^{\circ}$ meant that the binding process occurs spontaneously under the experimental conditions. In cephalothin-BSA complex formation, since the net enthalpy change value and entropy change value are positive, it is assumed that hydrophobic bindings are predominant in this binding process.

  • PDF

Drug-Biomacromolecule Interaction VIII

  • Kim, Chong-Kook;Yang, Ji-Sun;Lim, Yun-Su
    • Archives of Pharmacal Research
    • /
    • 제7권2호
    • /
    • pp.87-93
    • /
    • 1984
  • The effects of ionic strength and pH on the binding of cefazolin to bovine serum albumin (BSA) were studied by UV difference spectrophotometry. As ionic strength at constant pH and temperature increases, the apparent bining constant decreased but the number of binding sites remained almost constant at 2. The constancy of the number of binding sites with increasing the ionic strength suggests that purely electrostatic forces between BSA and drug do not have great importance in the drug binding, even though there is a decrease in the apparent binding constant. Thus, the effect of ionic strength on the interaction between drug and BSA may be explained by the changes in ionic atmosphere of the aggregated BSA molecules and competitive inhibition by phosphate ions. In addition, the higher apparent binding constant at high ionic strength is explained by conformational changes of BSA from its aggregate forms into subunits. The pH effects on the afinity of interactions indicated that the binding affinity of cefazoline is higher in the neutral region than in the alkaline region. An d at high pH value, the number of binding sites decreased from 2 to 1 because of the conformational change of BSA in the alkaline region.

  • PDF

Studies on the Interaction of Edible Dyes with Protein (II). The effects of drug additions on protein binding of edible dyes

  • Kim, Bak-Kwang;Lah, Woon-Lyong;Jang, Seong-Ki;Lim, Bang-Ho;Jang, Jae-Yeon;Lee, Wang-Kyu
    • Archives of Pharmacal Research
    • /
    • 제10권1호
    • /
    • pp.29-35
    • /
    • 1987
  • The effect of drug addition on the bovine serum albumin (BSA)-edible dye complex was studied by spectrophotometric method. The edible dyes tested were amranth, erythrosine, tatrazine and sunset yellow. The moles of bound dye per protein mole and free energies for edible dyes bounded were determined at pH 7.4. The values of free energy change by the addition of drughs to BSA-edible dye were ranged fro -6, 260 to 08030 cal/mole. In the wide range of edible dye concentration (0.3-$7{\times}10^{-5}$$^{-5}$ M), acetylsalicylic acid (ASA) showed pattern of displacement different from that of dye. It was assumed that ASA has different binding mechanisms from edible dye.

  • PDF

막성신염방(膜性腎炎方)이 Cationized Bovine Serum Albumin투여로 유발된 Mouse의 Membranous Nephropathy에 미치는 영향 (A Study for Effects of Magsungsinyeom-bang(Moxingshenyanfang) on Membranous Nephropathy induced by Cationic Bovine Serum Albuminin in Mouse Model(Effects of Magsungsinyeom-bang on Membranous Nephropathy))

  • 김재형;조충식;김철중
    • Korean Journal of Acupuncture
    • /
    • 제24권4호
    • /
    • pp.163-180
    • /
    • 2007
  • Objective : Oriental medicines have been applied to Membranous nephropathy(MN) for the purpose on increasing renal blood flow and modulating immune activity in according to Oriental medicine theories. Magsungsinyeom-bang (MSSYB) is one of the prescription which is known to show positive results in clinic with lack of laboratorial evidence. Thus, this study was aimed to evaluate the effects of MSSYB and partially investigate the mechanisms of it. Methods : The effect of MSSYB was evaluated by the morphology for the GBM thickening, protein excretion in urine and biochemical parameters in serum using cBSA-induced MN mice model. Mice were administered with MSSYB(250 or 500 mg/kg) or PBS for control group from experimental week 3 for 4 weeks. Results : 24 hrs proteinuria and the concentrations BUN was significantly decreased in the MS groups compared to the control group while the concentrations of serum albumin was higher in the MS groups than control group. MSSYB didn't affect the ratio of CD3e+/CD or 19CD4+/CD8 in the spleen and kidney, but inhibit the expression of IL-1${\beta}$, TNF-${\alpha}$, IL-6, and production of IgG and IgM. In histological analysis of kidney tissue, thickening of GBM was significantly decreased in the MS group compared to control group. Conclusions : MSSYB showed the positive results on the cBSA-induced membranous nephropathy in mice, thus, it could be a useful candidate for oriental drug for treating the membranous nephropathy in clinic.

  • PDF