• Journal of Gastric Cancer
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• 제5권2호
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• pp.106-112
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• 2005

목적: 영양상태가 면역력과 상관관계가 있다는 점에 착안하여 위암 환자에서의 혈청 알부민수치와 림프구아형의 수적인 병화에 근거하여 그 상관관계를 확인하고자 본 연구를 시행하였다. 대상 및 방법: 1998년 8월부터 2004년 8월까지 위암으로 진단 받고 수술을 시행한 한자 중에서 수술 전에 말초혈액 림프구아형 검사를 시행한 환자 150명을 대상으로 하였다. 결과: 위암 환자에서 혈청 알부민수치 변화에 따른 림프구아형의 병화를 비교하였고, 각 병기에 따른 변화도 비교하였다. 3.2 mg/dl를 기준으로 환자들을 구분하였을 때 말초혈액 림프구수, CD3+ 세포, CD4+ 세포, CD8+ 세포, CD16+56 세포수는 혈청 알부민 수치가 3.2 mg/dl 이상인 군보다 3.2 mg/dl 미만인 군에서 의미 있게 감소한 것을 볼 수 있었다(P<0.05). 혈청 알부민수치가 낮은 군에서 제1기(n=59)에서는 CD16+ 세포수의 감소, CD4+/CD8+ 비율의 의미 있는 증가가 있었다(P<0.05). 제IV기(n=33)에서도 혈청 알부민수치가 낮은 군에서 CD19+세포를 제외한 나머지 모든 림프구아형의 수적인 감소가 있었고 CD4+/CD8+ 비율의 증가가 있었다(P<0.05). 결론: 혈청알부민수치가 낮은 군이 정상인 군보다 전반적인 림프구아형의 절대수가 낮다. 이에 근거하여 위암 환자에서 영양상태와 면역상태는 깊은 상관관계가 있음을 다시 확인하였다.

• 대한수의학회지
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• 제8권1호
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• pp.45-53
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• 1968

1. The albumin, ${\beta}-globurin$ and ${\gamma}-globurin$ fractions of non-vaccinated bovine serum (Control) int declined, and a total protein and ${\alpha}-globurin$ level are advanced on the reversible rather than of vaccinated immumized bovine serum. (Table 5.) 2. Some few exists the to bring about changed in the individuals and sexual in a vaccinated bovine serum, however, Male serum globurin fractions are higher than Female globurin fractions percentage. (Table 1 and 3.) 3. Albumin fractions are Age-ablly variable, so that, younger's are rather lower than adult's such reported as in the another litratures. 4. In the monthly analysis of immunized bovine serum the first week to at dulation for third weeks were slowly advanced as variablly in serum-protein fractions of ater by the Black-leg No. 2 vaccination, then, albumin fractions were illustated as maximum ratio (42.73 3.49%) and increased much as 14.9% more than non-vaccinates, and ${\alpha}-globurin$ fractions indicated the minimum ratio(15.11 2.35%) at for 4th month after vaccination decrease much as about 7.71 % rather non-vaccinated normal bovine serum. (Table 4. and Fig 3.) Next, continuous advanced the ${\beta}-globurin$ fractions at first month as primary crisis in a diagram, and indicated the maximum ratio at 8th months as the second crieir on the its diagram of after vaccinati on, however, few changed in non-vaccinated bovine serum. (Figs 4.) Especially, ${\gamma}-globurin$ fractions are advanced the maximum ratio as 41. 45% 4.48% anp advanced to be widely range much as about 22.55% more than control serum at 5th months of after the vaccination. That is one of the most considerable evalution in Black-leg No. 2 vaccination to Korean calevs as great presence of the maximum immune antibodies at for 5th month after the vaccination. (Table 4. and Fig 4.) 5. In the relationship between vaccinated rabbit and Korean calves, serum protein fraractions were to be changed within the 3 weeks, so that albumin fractions of vaccinated immune bovine serum are increased as directly ratio, while vaccinated rabbit immunized serum showed the decrease as to reciprocal ratio. Although, conclude that ${\gamma}-globurin$ fractions are increased gradually by and large on the vaccinated immune bovine serum(B. P. S.) and vaccinated immune rabbit serum(R. P. S.) together. (Table 6).

• Archives of Pharmacal Research
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• 제19권4호
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• pp.269-274
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• 1996

The binding interactions between human serum albumin (HSA) and the edible food dyes amaranth, tartrazine and sunset yellow have been studied. Intrinsic association constants and the free energy changes associated with dye-protein binding at physiological pH for amaranth and tartrazine, and at two different pH values for sunset yellow have been calculated from ultrafiltration data. The temperature dependence $(20-40^{\circ}C)$ of the intrinsic association constants at pH 7.4 for amaranth-HSA and tartrazine-HSA mixtures have been measured, from which a plot of the van't Hoff isochore exhibits a marked change in slope around $30^{\circ}C$ indicating a possible change in protein conformation. The number of dye binding sites on HSA is reported for all the above conditions. HSA-ligand binding enthalpies have been used in conjunction with the N-B transitional binding enthalpy for HSA, to calculate the enthalpy for the N-B transition when ligands are bound with the protein.

• Bulletin of the Korean Chemical Society
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• 제35권9호
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• pp.2621-2624
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• 2014

The rapid and spontaneous adsorption of proteins on nanoparticle (NP) surfaces in biological fluids such as blood is an important phenomenon as it possibly determines "what the cells see" and, thus, the fates of NPs in living organisms. In order to quantitatively understand protein coronas at the molecular level, we investigated human serum albumin (HSA) coronas that were produced on silica NPs of 20 nm and 50 nm diameters using conventional gel electrophoresis. Analysis of the concentration dependence of protein adsorption showed that HSA coronas preferentially formed a monolayer on silica NPs and revealed the presence of hard protein coronas. HSA adsorption was clearly dependent on NP size, and this might be due to the different surface curvatures of NPs of different sizes.

• Journal of Applied Biological Chemistry
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• 제57권1호
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• pp.33-40
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• 2014

Polysaccharides have attracted great attention for their wide range of applications in biological and medical fields. In this paper, the interaction of polysaccharides with human serum albumin (HSA) was systematically investigated by fluorescence (FL) spectroscopy and circular dichroism (CD) spectra under different conditions. The Stern-Volmer quenching constants ($K_a$) at different ionic strength and pH were calculated, and information of the structural features of HSA was discussed. FL and CD results indicate that both hydrophobic and electrostatic interactions play important roles during the binding process. The quenching of the fluorescence resulting the binding of polysaccharides and HSA is static.

• 동아시아식생활학회지
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• 제7권1호
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• pp.1-11
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• 1997

The purpose of this study was to describe the protein nutritional status of female collegians between nonvegetarian diet groups(14) and vegetarian diet groups(19). Daily intake, protein were calculated from food direct measurement. Urea/creatinine, muscle mass, fatique conditions and hematological parameter were calculated. Blood samples were analyzed for total protein, albumin ammonia, urea, uric acid, creatinine, BUN contents. The results obtained are summarized as following : 1) On total dietary intake, especially Fe, vitamin C, niacin intake, vegetarian groups were higher than non vegetarian groups. 2) On composition of EAA(essential amino acids), vegetarians were highter than non vegetarian of leucine contents, but were lower lysine and threonine contents. 3) On urea / creatinine excretion, vegetarians were higher than non begetarians. Muscle mass were non signicant, fatique condition, vegetarians were normal state. 4) Non vegetarians were increased serum albumin total protein, uric acid, ammonia but vegetarians were decreased BUN, ammonia after experimental diet intake. 5) In process of time after meal, non vegetarians were increased serum albumin total protein, BUN, but vegetarians were decreased ammonia.

• Journal of Photoscience
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• 제11권2호
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• pp.65-69
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• 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.

• Journal of Photoscience
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• 제12권3호
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• pp.113-117
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• 2005

Spectroscopic investigations on the interaction of gabapentin (GBP) with bovine serum albumin (BSA) were reported. The association constant of GBP-BSA system was determined at different temperatures (298, 302, 306 and 311 K) based on the fluorescence quenching results. The GBP was found to quench the fluorescence of BSA through static mechanism. Thermodynamic parameters, the standard enthalpy change, $({\Delta}H^o)$ and the standard entropy change $({\Delta}S^o)$ were observed to be $-9.61{\pm}0.008\;kJ\;mol^{-1}$ and $3.58{\pm}0.011\;Jmol^{-1}K{-1}$ respectively. These indicated that the hydrophobic and electrostatic forces played a role in the interaction of GBP with BSA. The negative value of ${\Delta}G^o$ revealed that the binding reaction is spontaneous. The circular dichroism studies indicated the conformational changes in BSA upon interaction with GBP. The effect of some metal ions on the binding constant was also investigated.

• Bulletin of the Korean Chemical Society
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• 제30권6호
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• pp.1262-1266
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• 2009

Thermodynamics of the interaction between Cerium (III) chloride, $Ce^{3+}$, with Human Serum Albumin, HSA, was investigated at pH 7.0 and $27\;{^{\circ}C}$ in phosphate buffer by isothermal titration calorimetry. Our recently solvation model was used to reproduce the enthalpies of HSA interaction by $Ce^{3+}$. The solvation parameters recovered from our new model, attributed to the structural change of HSA and its biological activity. The interaction of HSA with $Ce^{3+}$ showed a set of two binding sites with negative cooperativity. $Ce^{3+}$ interacts with multiple sites on HSA affecting its biochemical and biophysical properties.

• 약학회지
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• 제26권2호
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• pp.85-90
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• 1982

The binding of the 1-anilinonaphthalene-8-sulfonate(ANS) to bovine serum albumin was studied by fluorescence spectroscopy. The effect of pH, ionic strength, and protein concentration on the binding of ANS to protein were compared. The binding between ANS and protein was dependent on pH and ionic strength. It seems that both hydrophobic binding and some electrostatic forces are involved in the binding of ANS to protein. The binding constants for ANS increased with increasing protein concentration. This suggests the possibility of a sharing of one ANS molecule by more than one protein molecule at relatively high protein concentration.