• 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.

• Archives of Pharmacal Research
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• v.12 no.3
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• pp.160-165
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• 1989

Binding of sulfaethidole to bovine serum albumin was studied by equilibrium dialysis, fluorescence probe technique, uv difference spectrophotometry and circular dichroism. Equilibrium dialysis method enabled us to estimate the total number of drug binding sites of albumin molecule. For sulfaethidole, albumin had 6 primary and 40 secondary binding sites. The primary and secondary binding constants were 0.9 * 10/sup 5/ M/sup -1/ and 0.2 * 10/sup 6/ M/sup -1/, respectivitely. 1-Anilino-8-naphthalenesulfonate (ANS) and 2-(4-hydroxylbenzeneazo)- benzoic acid (HBAB) were used as the fluorescence probe and the uv spectrophotometric probe, respectively. In fluorescence probe technique, results indicated that the number of higher affinity drug binding site of albumin was 1 and the number of lower affinity drug binding sites of albumin was 3, and the primary and secondary drug binding constants for bovine serum albumin were 2.15 * 10/sup 5/M/sup -1/ and 1.04 * 10/sup 5/ M/sup -1/, respectively. In uv difference spectrophotometry, binding sites were 3 and binding constant was 1.88 * 10/sup 5/M/sup -1/. The above spectrophotometry, binding sites were 3 and binding constant was 1.88 * 10/sup 5/M/sup -1/. The above results suggest that several different methods should be used in ompensation for insufficient information about drug binding to albumin molecule given by only one method.

• Journal of Chest Surgery
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• v.22 no.6
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• pp.921-926
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• 1989

The Free fatty acid [FFA] induced massive erythrocyte crenation has been reported in patients undergoing extracorporeal circulation[EGG], suggesting that the crenated cells impair microcirculatory flow and tissue oxygenation during and after the operation. Effect of albumin administration on erythrocyte crenation was examined in 24patients undergoing open heart surgery at the department of Thoracic and Cardiovascular Surgery in the Kyung Hee University Medical Center Between January, 1989 and August, 1989: 8 patients of 24 patients [group A] were given 50 gm albumin, another 8 patients of 24 patients [group B] were g en 26 gm of albumin and the other 8 patients of 24 patients [group C] were not given any albumin as a part of the priming solution. Erythrocyte crenation was almost completely prevented in the patients given 50 gm albumin. Crenated erythrocytes d urging ECC were 3.6* 0.4 % [mean\ulcornerD] of all erythrocytes and 3.1*0.6% after ECC. This was significantly lower than in patients without albumin administration [64.2*9.5% during ECC and 28.7*1.9% after ECC]. But the effect was less striking in the patients given 25 gm albumin, 37.8* 12.0 % during ECC and 27.8*3.9 % after ECC. Maintaining an adequate level of plasma albumin is important in preventing erythrocyte crenation during ECC, improving microcirculatory flow in patients undergoing open heart surgery.

• The Korean Journal of Pharmacology
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• v.31 no.1 s.57
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• pp.135-140
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• 1995

Glycation occurs by covalent binding between the carbonyl group of monosaccharides and the epsilon amino group of amino acid. It can alter the physiological function of proteins and causes the development of diabetic complications. In this study, the influence of glycation on protein binding of warfarin and dansylsarcosine was studied by equilibrium dialysis which was performed for 3 hours at $37^{\circ}C$ in the water bath. The high glycated albumin which contained $50{\pm}16%$ of glycated albumin bound less than natural albumin which contained $8.5{\pm}5.28%$ of glycated albumin, if drugs concentration were more than the albumin concentration. But only warfarin binding showed a significant difference of 6% (P<0.05) when the molar concentration ratio of warfarin per albumin was 3. In consideration of low therapeutic concentrations, low glycated albumin concentrations in the body, and rapid elimination of excessive free drugs, these small increaes of free warfarin concentrations by glycation of albumin are not considered as risk. factors for drug intoxication for diabetics, if renal functions are intact.

• The Korean Journal of Food And Nutrition
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• v.13 no.3
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• pp.242-248
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• 2000

수산물 가공시 흘러나오는 폐수 중에 함유되어 있는 수용성 단백질을 chitosan에 흡착시키기 위하여 albumin과 hemoglobin, albumin-myoglobin 혼합단백질을 이용하여 chitosan과의 흡착 및 chitosan 제조조건에 따른 흡착효과와 chitosan의 수용성 단백질 흡착에 미치는 인자를 살펴본 결과는 다음과 같다. Chitosan위 탈아세틸화 조건을 60, 70, 80%로 달리하여, albumin, hemoglobin, albumin-myoglobin 혼합용액에 적용했을때 chitosan의 탈아세틸화도가 높을수록 chitosan과 단백질 사이의 흡착률은 높게 나타났다. 초음파 처리에 의하여 chitosan의 분자량이 작을수록 chitosan과 단백질 사이의 흡착률은 높게 나타났다. pH변화에 따른 chitosan과 수용성 단백질의 흡착률은 albumin 및 albumin-myoglobin 혼합용액에서는 pH 4.0에서, hemoglobin용액에서는 pH 7.0에서 흡착률이 높게 나타났다 chitosan과 수용성단백질과의 흡착에서 반응시간은 albumin및 albumin-myoglobin 혼합용액에서는 4시간, hemoglobin용액에서는 3시간까지 흡착률이 증가하였고, 그 이후의 시간이 경화하여도 흡착률의 증가는 거의 보이지 않았다. 수용성 단백질 용액에 NaCl 농도를 0.1M에서 1.0M로 증가시켜 첨가했을때 염의 농도가 높을수록 chitosan과 단백질 사이의 흡착이 잘 일어나지 않았다.

• Journal of Pharmaceutical Investigation
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• v.20 no.4
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• pp.179-191
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• 1990

A central dogma of pharmacology is that only unbound drug is capable of translocation across biological membrane. Thus, hepatic uptake is assumed to be solely determined by the unbound concentration of the diffusible moiety at the surface of the liver cell. However, an increasing number of experimental observations with xenobiotics that are normally very extensively bound to plasma proteins (>99%) appear to be inconsistent with these assumptions. This suggested that in addition to progressive spontaneous dissociation within the liver sinusoids and space of Disse, direct interactions of the albumin-drug complex at the plasma membrane may facilitate dissociation of the complex. To explain this phenomena. called albumin-mediated uptake, 4 mechanisms have been suggested. The validity of such hypotheses needs to be examined by the further study. Because albumin-mediated uptake has also been observed to occur in other plasma proteins, protein-mediated uptake rather than albumin-mediated uptake seems to be acceptable.

• Korean Journal of Veterinary Research
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• v.15 no.1
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• pp.19-22
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• 1975

The serum albumin phenotypes and the gene frquencies of 100 Korean native goats were examined by starch gel electrohporesis. The results obtained were as follows: 1. The albumin phenotypes were classified as Alb AA, Alb AB, and Alb BB and the frequencies of appearence were 10, 12 and 78%, respectively. 2. The genetic factors of serum albumin were observed as Alb A and Alb B and the rates of gene frequencies were 16 and 84%, respectively.

• The Korean Journal of Pharmacology
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• v.30 no.2
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• pp.255-260
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• 1994

There are some reports about the influences of free fatty acids on the albumin binding of drugs. But they were concerned to the limited free fatty acids, mostly of azapropazone-warfarin bidning site bound drugs and determination of dissociation and association constants by stopped flow technique. These data were not enough to make conculsions for the general tendency of free fatty acid to albumin binding. Therefore the influence of various saturated fatty acids of $C_{10{\sim}20}$, oleic acid and linoleic acid as unsaturated fatty acids to albumin binding of warfarin and dansylsarcosine were studied by equilibrium dialysis. The concentration of free drug was determined by spectrophotometer according to the molar ratios of 0, 0.5, 1, 2 and 4 between free fatty acid and albumin. There were significant increasing in the free durg concentration of warfarin and dansylsarcosine when the molar ratio for capric acid, lauric acid and palmitic acid was 4. The free warfarin concentration was increased significantly at a molar ratio of 4 between oleic acid and albumin. Therefore the albumin binding of durgs can be variated significantly by increased free fatty acid of diabetics and cause to the pharmacokinetic variation between healthy and diabetics.

• 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, $1.21{\times}10^{3}M^{-1}$.

• Journal of Veterinary Clinics
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• v.36 no.3
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• pp.145-149
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• 2019

Previous report has suggested that the albumin levels were reduced in the peripheral blood mononuclear cells (PBMCs) and consequently oxidative stress was elevated in streptozotocin (STZ)-induced diabetic rats as albumin is the predominant antioxidant in plasma. In this study, we suggest that the levels of pro-inflammatory cytokine such as interleukin-6 (IL-6) and tumor necrosis factor-${\alpha}$ ($TNF-{\alpha}$) were increased by approximately 3.4- and 2.9-fold, respectively, in the serum of STZ-diabetic rats, compared to those of normal rat. In addition to the cytokines, the levels of C-reactive protein (CRP) were also about 3.6-fold higher, indicating that STZ induced a pro-inflammatory response in rat blood. However, when purified rat albumin was externally co-administrated with STZ through the tail vein, the serum levels of IL-6, $TNF-{\alpha}$, and CRP were markedly reduced, although the values were still higher than those of normal (non-diabetic) rats. Albumin administration also decreased STZ-induced oxidative stress in serum and PBMCs. Moreover, the decrease in cytokine and CRP levels was dependent on the dose of injected albumin. These results suggest that STZ-induced pro-inflammation and oxidative stress in rat blood might be attenuated by treatment with exogenous albumin.