No abstract available.
Serum Albumin ; Track and Field

Consensus ; Critical Illness ; Humans ; Serum Albumin ; Serum Albumin, Human

No abstract available.
Embryonic Development* ; Female ; Humans* ; Pregnancy ; Serum Albumin*

PURPOSE: To correlate CT attenuation and MR signal intensity with concentration of protein solution. MATERIALS AND METHODS: CT and MR examinations of a phantom containing bovine serum albumin solutions of various concentrations ranging from 0 to 55% were performed. CT Hounsfield units(HUs), MR signal intensities, and apparent diffusion coefficients (ADCs) of each albumin solution were measured, and CT HUs and MR signal intensities of the solutions were compared with those of cerebrospinal fluid (CSF), white matter, and cortical gray matter. RESULTS: CT HU increased gradually with increasing albumin concentration. On T1-weighted images(T1WI), signal intensity increased with increasing albumin concentrations of up to 35% but then decreased. On T2-weighted images(T2WI), gradually decreasing signal intensity and increasing albumin concentration were oibserved. Fluid-attenuated inversion recovery (FLAIR) and diffusion-weighted images (DWIs) showed that signal intensity peaked at a concentration of 10% and then gradually decreased. The ADC of the solution gradually decreased as concentration increased. Compared with those of normal brain structures, the CT HUs of solutions at concentrations of over 20% were higher than those of white and gray matter. At T1WI, the signal intensities of 10-45% solutions were similar to or higher than that of the gray matter. At T2WI, the signal intensities of solutions above 25, 35, and 40% were lower than those of CSF, gray matter, and white matter, respectively. FLAIR images showed that the signal intensities of 5-35% solutions were higher than that of gray matter. CONCLUSION: The CT attenuation of albumin solution increased gradually with increasing concentration. MR signal intensities peaked at 35% concentration on T1WI and at 10% on FLAIR and DW images, respectively, and then gradually decreased. T2WI and ADC map images showed gradually decreasing signal intensity and ADC as albumin concentration increased.
Brain ; Cerebrospinal Fluid ; Diffusion ; Serum Albumin, Bovine

Recent studies showed that high biocompatibility and reduction of uremic toxin contributed to the improvement of freatment outcome in hemodialysis patients.Therefore, a high-flux membrane dialyzer, especially polysulfone (PS) membrane, was generally used in dialysis. However, it was suggested that the higher efficiency of reduction in uremic toxins might cause an increase in the albumin leakage through the dialyzer membrane during dialysis, resulting in a decrease in serum albumin concentration. In this study, we used two different dialyzer membranes with high biocompatibility, namely, ethylenevinylalcohol (EVAL) membrane and improved PS membrane with a very lower leakage of serum albumin. After using these two types of mambrane of six straight months, we examined the effect of each dialyzer membrane characteristic on the serum total protein and albumin concentration. The reduction rates of each uremic solute and serum total protein concentration were significantly higher. The serum albumin concentration and its rate of change with the passing of time tended to increase in the case of the PS membrane. But in the case of EVAL membrane, these values tended to decrease. These results suggested that the differences in the changes in the serum total protein and albumin concentration might result from the differences in the efficiency of the reduction of uremic toxins. Therefore, it is necessary to consider the usage of the dialyzer membrane with a higher reduction of uremic solutes and a lower leakage of serum albumin to add to the higher biocompatibility specially in hemodialysis patients with hypoproteinemia.
Membranes ; Concentration ; Reduction (chemical) ; Serum Albumin ; Hemodialysis

PURPOSE: To develop optimal microbubble contrast agents (MBCAs) for performing ultrasound microscopy when examining small animals. MATERIALS AND METHODS: We prepared three types of MBCAs. First, a mixture of three parts of 40% dextran and one part of 5% human serum albumin were sonicated with perfluorocarbon (PFC) (MB1-D40A5P). Second, three parts of 40% dextran and one part of 1% human serum albumin were sonicated with PFC (MB2-D40A1P). Third, all parts of 1% bovine serum albumin were sonicated with PFC (MB3-A1P). We measured the microbubbles' sizes and concentrations with using image analysis software. The acoustic properties of the microbubbles were assessed both in vitro and in vivo. RESULTS: The majority of the MB1-D40A5Ps had a diameter of 2-5 um, the mean diameter of the MB2-D40A1Ps was 2.5 um, and the mean diameter of the MB3-A1Ps was less than 2.0 um. Among the microbubbles, the MB1-D40A5Ps and MB2-D40A1Ps showed increased echogenicity in the abdominal vessels, but the duration of their contrast effect was less than 30 sec. On the contrary, the MB3-A1Ps exhibited strong enhancement in the vessels and their duration was greater than 120 sec. CONCLUSION: A microbubble contrast agent consisting of all parts of 1% serum albumin sonicated with PFC is an effective contrast agent for ultrasound microscopy.
Acoustics ; Animals ; Contrast Media* ; Dextrans ; Humans ; Microbubbles* ; Microscopy* ; Microspheres ; Serum Albumin ; Serum Albumin, Bovine ; Ultrasonography*

BACKGROUND: Generation of perfluorocarbon-exposed sonicated dextrose albumin (PESDA), the custom-made contrast agent, is performed under certain conditions that have been proposed by its original developer. We doubted whether the known composition and manufacturing method of PESDA is ideal and if there is an optimal method of storing batches of PESDA for a significant time duration. METHODS: PESDA was generated with several different composition of ingredients (5% human serum albumin, 5% dextrose water, and perfluorocarbon (PFC) gas), where various ratios of each were used. Sonication was performed for various durations. After manufacturing, the mean size and concentration of the microbubbles were evaluated by hemocytometer and compared. The generated PESDA was stored for 48 hours under 4 degrees C or -20 degrees C and changes in size and concentration of microbubbles were evaluated and compared. RESULTS: The best concentration of microbubbles was found with a mix ratio of albumin: PFC: dextrose of 1:1:1 and sonication time of 90 sec. The microbubble concentration of the optimal PESDA was not different to that of the conventionally manufactured one (9.47+/-1.70 x 10(8) /mL vs. 8.34+/-0.87 x 10(8) /mL, p>0.05) but the mean microbubble size was significantly smaller (1.22+/-0.31 um vs. 1.66+/-0.32 um, p<0.01). After 48 hours, the concentration of microbubbles was reduced by 34+/-3% (p=NS) and 55+/-0.2% (p<0.05) and the size increased by 77+/-25% and 108+/-41% (p=NS in both) in the 4 degrees C -stored and -20 degrees C -stored PESDA, respectively. CONCLUSION: The optimal composition of PESDA ingredients is 1:1:1 for albumin, PFC, and dextrose water, and the best duration of sonication is 90 seconds. Refrigeration under 4 degrees C may be the best way for storage of PESDA for 48 hours.
Echocardiography ; Glucose* ; Humans ; Microbubbles ; Refrigeration ; Serum Albumin ; Sonication ; Water

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 >or=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.
Humans ; Lymphocyte Subsets* ; Lymphocytes* ; Serum Albumin* ; Stomach Neoplasms*

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 >or=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.
Humans ; Lymphocyte Subsets* ; Lymphocytes* ; Serum Albumin* ; Stomach Neoplasms*

PURPOSE: Allergen extracts from the house dust mite (HDM, Dermatophagoides pteronyssinus) are widely utilized for diagnosis and treatment of allergic diseases. It is known that allergen extracts degrade and lose potency when stored over time. METHODS: This study aimed to determine the optimal conditions for stability of allergen extracts. This study was undertaken to investigate the optimal storage conditions for HDM extracts, the effects of adding 0.03% human serum albumin (HSA) and 50% glycerol were evaluated at -20degrees C, 4degrees C, and room temperature (RT). Changes in protein and group 1 major allergen (Der p 1) concentration, as well as allergenicity were measured over a 1 year period using the Bradford assay, two-site ELISA, and ELISA inhibition. RESULTS: Protein concentrations decreased by 86%, 51%, and 6% at RT, 4degrees C, and -20degrees C, respectively, when stored in distilled water. Overall allergenicity remained high (89.9%) when the extracts was reconstituted in 50% glycerol solution, and was 93.1% when reconstituted in 50% glycerol and 0.03% HSA at RT. Allergenicity was decreased to 36.6% and 33.3%, however, reconstitution in DW or 0.03% HSA solution at RT, respectively. Allergenicity was remained high as 92.0%-97.0% when stored at 4degrees C regardless of the buffer conditions. CONCLUSIONS: Storage temperature is the most important factor in preserving allergenicity of HDM extracts, which is ideal at 4degrees C. The addition of 50% glycerol to the storage buffer was also found to play an important role in increasing the shelf-life of HDM extracts at RT.
Enzyme-Linked Immunosorbent Assay ; Glycerol ; Humans ; Pyroglyphidae ; Serum Albumin ; Water