• Journal of the Korean Society of Food Science and Nutrition
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• v.23 no.3
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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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• v.1
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• pp.48-54
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• 1960

Studing the binding of the 5-Iodopyrimdines by human serum albumin we obtained the following conclusions; 1. The more strong electron donating groups in the molecule of 5-Iodopyrimidines, the larger the binding force with human serum albumin. This trend seems to be attributed by increase of polarization of the electron donating groups in 5-Iodopyrimidines molecule. 2. The binding force of 5-Iodopyrimidines by human serum albumin is increased with the pH increasing could be occurred the configurational changes of human albumin molecule, and this new binding sites of human serum albumin molecule would form the intermolecular complex with 5-Iodopyrimidines molecule more strongly.

• YAKHAK HOEJI
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• v.25 no.4
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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, $1.21{\times}10^{3}M^{-1}$.

• 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.

• Archives of Pharmacal Research
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• v.7 no.1
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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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• v.4 no.1
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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.

• 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.

• The Korean Journal of Mycology
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• v.6 no.2
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• pp.15-18
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• 1978

The study was performed to investigate the inhibitory action on the growth rate of Candida albicans under the various immunological conditions, Candida albicans was grown in broth media containing 0.1ml. (in total broth volume 4.0ml.) of normal human serum, diabetic patient serum, albumin solution, artifical bulla content and nutrient solution as control subject. The inhibitory action of Candida albicans was indicated by mesurement of transparency rate with use of the spectrophotometer. The results are as follows: 1. Normal human serum shows inhibitory effect on the growth of the candida distinctly. 2. Albumin solution reveals almost similar to that of the effect of normal human serum. 3. Artificial bulla content which obtained by irradiation of ultraviolot ray after application of 1% 8-Methoxy-psolaren cream and the diabetic patient serum shows reduction of inhibitory effect as compared with that of the normal human serum. 4. It is estimated that the titer of negative effect of diabetic patient serum is not related with the variation of immunoglobulin titer in patient serum.

• Journal of Radiopharmaceuticals and Molecular Probes
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• v.4 no.2
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• pp.85-89
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• 2018

We demonstrate a detail protocol for the radiosynthesis of an $^{125}I$-labeled MSTP prosthetic group and its application to the efficient radiolabeling of human serum albumin (HSA). Radioiodination of the precursor (2) was carried out by using $[^{125}I]$NaI and chloramine T as an oxidant at room temperature for 15 min. After HPLC purification of the crude product, the purified $^{125}I$-labeled MSTP ($[^{125}I]1$) was obtained with high radiochemical yield ($73{\pm}5%$, n = 3) and excellent radiochemical purity (>99%). Site-specific reaction between ($[^{125}I]1$) and HSA gave the $^{125}I$-labeled human serum albumin ($[^{125}I]3$) with more than 99% of radiochemical yield as determined by radio-thin-layer chromatography (radio-TLC). These results clearly demonstrate that the present radiolabeling method will be useful for the efficient and convenient radiolabeling of thiol-bearing biomolecules.

• 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.