• 한국식품영양과학회지
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• 제23권3호
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• pp.414-419
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• 1994

This study was trying to find what physical changes occurred to albumin when it reacted with estrogen and other ligands. Each concentration of human serum albumin with 100$\mu$l estradiol reacted at the highest binding capacity of 280nm. In addition, 1 hr of reaction time showed the highest binding rate. Conformational changes in human serum albumin with dietylstillbesterol and N-ethyl-maleimide produced strong binding capacities. The changes were immediate and they did not increase or decrease over time. Effects of human serum albumin with estriol induced no interaction each other. The binding capacity of human serum albumin with vitamin D$_2$was lower than estradiol. and the highest binding rate showed 1 hr of reaction time. Vitamin D$_2$ was very similar to the binding capacity of estradiol.

• Applied Biological Chemistry
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• 제1권
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• pp.48-54
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• 1960

5-Iodopyrimidines와 Human serum albumin 간(間)의 결합(結合)에 있어 이들의 결합량(結合量)은 첫째 5-Iodopyrimidines 분자내(分子內) Iodine에 대(對)한 Introducing group이 변(變)함에 따라 변(變)하게 된다. 다시 말해서 결합량(結合量)은 5-Iodopyrimidines 분자내(分子內) 보다 강(强)한 electron donating group이 존재(存在) 함에 따라 한층 더 증가하게 된다고 말할 수 있다. 둘째 이들 두 물질간(物質間)의 결합량(結合量)은 또한 PH 증가에 따라서도 증가한다고 말할 수 있는데 이는 PH 증가에 따라 Human serum albumin 분자자체내(分子自體內)의 Configuration이 변(變)하게 됨으로서 분자내(分子內) electrostatic repulsion에 의(依)한 새로운 결합부분(結合部分)이 증가될 것이며, 이 부분(部分)에서의 복합체(復合體)를 형성(形成)함에 기인(基因)한다고 생각된다. 이러한 실험적(實驗的) 결과(結果)를 토대로 하여 5-Iodopyrimidines가 antithyroid action과 어떠한 관계(關係)를 갖고 있는가의 실험(實驗)을 함으로서 결합량(結合量)에 따른 antithyroid activity 서열(序列)을 결정(決定)할 수도 있을 것이다.

• 약학회지
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• 제25권4호
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• pp.161-165
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• 1981

The binding of two cephalosporins, cephalothin and cefazoline to human serum albumin(HSA) was studied by difference spectrophotometry using a spectrophotometric probe, 2-(4'-hydroxybenzeneazo) benzoic acid. The probe is strong visible absorbing material which interacts with serum albumin to give characteristic spectrophotometric peaks and provides the basis for a convenient assay to measure free and bound amounts in the presence of serum albumin and competitive drugs. The results obtained showed that the probe and cephalosporin compete for the same binding site on human serum albumin; thus the probe can be used to gauge the displacement of cephalosporins from human serum albumin. The data were interpreted on the basis of theory of multiple equilibria. The number of binding sites of human serum albumin for 2-(4'-hydroxybenzeneazo) benzoic acid(HBAB), cephalothin and cefazoline appears to be 4. By using this technique the binding constants were found as follows: HSA-HBAB, $7.89{\times}10^{4}M^{-1}$; HSA-cephalothin, $1.09{\times}10^{3}M^{-1}$ ; HSA-cefazoline, $1.21{\times}10^{3}M^{-1}$.

• 한국미생물·생명공학회지
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• 제29권4호
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• pp.248-252
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• 2001

메탄올 자화효모 Hansenula polymorpha 가 생산하는 재조합 인체 알부민 (human albumin)을 heat treatment ultrafiltration phenyl Sepharose CL-4B Mono Q 컬럼 크로마토그래피를 수행하여 수율 60%로 정제하였다. 정제된 재보합 알부민 SDS-PAGE를 수행한 결과 분자량이 65,000 Da으로 나타났고, 본 재조합 알부민의 N-말단 아미노산 서열은 Asp- Ala- His- Lys- Ser- Glu- Ala 으로 혈청유래 알부민 및 다른 효모 유래의 재조합 인체 알부민 과 동일함을 보였다. 정제한 재조합 인체 알부민의 아미노산 조성은 총 18종 의 아미노산이 검출되었고 아미노산 잔기 중 cysteine, arginine lysine 등이 이론치와 일치하였으며, 혈청 알부민과 동일하게 약 pI 4.8 정도 값을 나타내어 H. polymorpha 유래의 재조합 단백질의 전반적인 아미노산 구성이 혈청 알부민과 동일함을 확인하였다.

• Archives of Pharmacal Research
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• 제7권1호
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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.

• Archives of Pharmacal Research
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• 제6권1호
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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.

• Nanomaterials
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• 제12권5호
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• pp.758-770
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• 2022

Parkinson's disease is one of the most common degenerative disorders and is characterized by observable motor dysfunction and the loss of dopaminergic neurons. In this study, we fabricated curcumin nanoparticles using human serum albumin as a nanocarrier. Encapsulating curcumin is beneficial to improving its aqueous solubility and bioavailability. The curcumin-loaded HSA nanoparticles were acquired in the particle size and at the zeta potential of 200 nm and -10 mV, respectively. The curcumin-loaded human serum albumin nanoparticles ameliorated Parkinson's disease features in the C. elegans model, including body movement, basal slowing response, and the degeneration of dopaminergic neurons. These results suggest that curcumin nanoparticles have potential as a medicinal nanomaterial for preventing the progression of Parkinson's disease.

• Biotechnology and Bioprocess Engineering:BBE
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• 제6권1호
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• pp.25-30
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• 2001

Viral safety is a prerequisite for manufacturing clinical albumin and immunoglobulins from human plasma pools. This study was designed to evaluate the efficacy of cold ethanol fractionation and pasteurization (60$\^{C}$ heat treatment for 10h) for the removal/inactivation of human immunodeficiency virus type 1 (HIV-1) during the manufacturing of albumin and immunoglobulins. Samples from the relevant stages of the production process were spiked with HIV-1, and the amount of virus in each fraction was quantified by the 50% tissue culture infectious dose(TCID(sub)50). Both fraction IV fractionation and pasteurization steps during albumin processing were robust and effective in inactivating HIV-1, titers of which were reduced from an initial 8.5 log(sub)10 TCID(sub)50 to undetectable levels. The log reduction factors achieved were $\geq$ 4.5 and $\geq$ 6.5, respectively. In addition, fraction III fractionation and pasteurization during immunoglobulins processing were robust and effective in eliminating HIV-1. HIV-1 titers were reduced from an initial 7.3 log(sub)10 TCID(sub)50 to undetectable levels. The log reduction factors achieved in this case were $\geq$ 4.9 and $\geq$ 5.3, respectively. These results indicate that the process investigated for the production of albumin and immunoglobulins have sufficient HIV-1 reducing capacity to achieve a high margin of safety.

• Archives of Pharmacal Research
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• 제4권1호
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• pp.19-24
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• 1981

The possibility of using a fluorescence probe technique for the study of ibuprofenlysine binding to human and bovine serum albumin was investigated. 1-anilino-8-naphalenesulfonate was used as the probe. The number of binding sites of human and bovine serum albumins for ibuprofenlysine appears to be 4 and 2, respectively. By using this technique, the association constants were found to be $1.533{\times}10^{4}M^{-1}$ and $2.238{\times}10^{4}M^{-1}$, respectively.

• Biotechnology and Bioprocess Engineering:BBE
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• 제9권1호
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• pp.65-68
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• 2004

The purpose of the present study was to examine the efficacy and mechanism of fraction IV cold ethanol fractionation and pasteurization (60$^{\circ}C$ heat treatment for 10 h), involved in the manufacture of albumin from human plasma, in the removal and/or inactivation of the hepatitis A virus (HAV). Samples from the relevant stages of the production process were spiked with HAV and the amount of virus in each fraction then quantified using a 50% tissue culture infectious dose (TCID$\_$50/). HAV was effectively partitioned from albumin during the fraction IV cold ethanol fractionation with a log reduction factor of 3.43. Pasteurization was also found to be a robust and effective step in inactivating HAV, where the titers were reduced from an initial titer of 7.60 log TCID$\_$50/ to undetectable levels within 5 h of treatment. The log reduction factor achieved during pasteurization was $\geq$4.76. Therefore, the current results indicate that the production process for albumin has sufficient HAV reducing capacity to achieve a high margin of virus safety.