• Journal of Gastric Cancer
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• v.5 no.2
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• pp.106-112
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• 2005

Purpose: Considering that nutritional state correlates to immunity, we performed this study to evaluate the correlation by assessing the numerical changes of the levels of serum albumin and lymphocyte subsets. Materials and Methods: The study was performed on patients who were diagnosed as having gastric cancer and who underwent curative surgery from August 1998 to August 2004 in the Gyeongsang National University Hospital and whose peripheral blood lymphocyte subsets were tested prior to surgery. The study population was a total of 150 cases. Results: The change in the lymphocyte subsets in relation to the change in the level of serum albumin in all patients with gastric cancer was determined, and was compared to disease stages. When patients were classified by using the level of serum albumin with 3.2 mg/dl as the cut-off point (low group: serum albumin <3.2 mg/dl, normal group = serum albumin $\geq$ 3.2 mg/dl), the number of peripheral blood lymphocytes, CD3+ cells, CD4+ cells, CD8+ cells, and CD16+ 56 cells were, significantly lower in the group with the level of serum albumin below 3.2 mg/dl (low group) than it was in the group with a serum albumin level above 3.2 mg/dl (normal group) (P<0.05). In stage I (n=59), CD16+56 cells were significantly lower in the low group. In stage II (n=29), the number of CD16+56 cells was lower and the ratio of CD4+/CD8+ was higher in the low group than in the normal group significantly. In stage IV (n=33), except for CD19+ cells, the number of all lymphocyte subsets was significantly lower and the ratio of CD4+/CD8+ was significantly higher in the low group. Conclusion: The group with a low level of serum albumin had a low absolute number of lymphocyte subsets. Based on this, we reconfirmed that the nutritional state is closely related with the immune state in patients with gastric cancer.

• Korean Journal of Veterinary Research
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• v.8 no.1
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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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• v.19 no.4
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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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• v.35 no.9
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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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• v.57 no.1
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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.

• Journal of the East Asian Society of Dietary Life
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• v.7 no.1
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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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• v.11 no.32
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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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• v.12 no.3
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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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• v.30 no.6
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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.

• YAKHAK HOEJI
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• v.26 no.2
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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.