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

OBJECTIVETo develop a best chitosan film for using as a drug sustained-release system through the evaluation of the sustained-release property, degradation property, and cytotoxicity to osteoblast.

METHODSOrthogonal experiments were designed to determine the best combination of chitosan film preparations. Drug release rate was determined with Coomassie brilliant blue G250. In a separate study, chitosan films were placed into the test tubes with buffer solution and 10(7) U/L lysozyme. The degradation rate was calculated. Osteoblasts derived from fetal rat calvarial were cultured on chitosan films. Cell proliferation was tested by methyl thiazolyl tetrazolium (MTT) assay. The relative growth rate was calculated and the cytotoxicity was graded.

RESULTSThe best processing condition was 1% acetic acid, chitosan concentration of 2 mg/mL, 6% sodium tripolyphosphate (STPP) concentration, and cross-linking time of one hour. The resulting chitosan film released 33.13% of bovine serum albumin (BSA) within 8 d, 36.73% of BSA within four weeks and the cytotoxicity grade was 0 or 1.

CONCLUSIONThis chitosan film possesses good sustained release property, and a good degradation rate.

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*

It was investigated if regulation of the trabecular extracellular matrix tumover rate and remodeling plays an important role in decreasing outflow resistance by determining the effect of intracamerally given interleukin-1alpha a known stimulator of the expression of trabecular matrix metallopro-teinases, on outflow facility of albino rat eyes. Forty normal albino rats (Sprague dawley) weighing 250 to 300gm were studied. Rats were anesthetized by intraperitoneal pentobarbital sodium(30mg/kg) injection. The rats were grouped into 4 groups and given 5, 10, 25, 50 units of interleukin-1alpha injected intracamerally in one eye of each rat. Bovine serum albumin in phosphate buffered saline, which was used to dissolve the interleukin-1alpha, was injected in the other eye as a control. Outflow facility was measured by two level constant pressure perfusion at 1, 3, and 7 days after injection. The eyes treated with 50 units of interleukin-1alpha showed a statistically significant increase of outflow facility by 37% compared to the contralateral control eyes at 3 days after injection, but retumed to normal level in 7 days. The eyes treated with 5, 10, 25, 50 units of interleukin-1alpha increased the outflow facility, supporting the hypothesis that regulation of trabecular meshwork extracellular matrix plays a role in trabecular outflow resistance.
Animals ; Extracellular Matrix ; Interleukin-1alpha* ; Interleukins ; Pentobarbital ; Perfusion ; Rats* ; Serum Albumin, Bovine ; Trabecular Meshwork

This study was performed to investigate the stimulating effect on oocyte maturation and cumulus cell expansion in TC199 media by human cord serum (HCS) supplementation. Immature mouse oocyte cumulus complexes (OCCs) were cultured in TC199 media supplemented with bovine serum albumin (BSA), HCS and human chorionic gonadotropin (hCG) instead of luteinizing hormone (LH) respectively, and the expression of cumulus expansion and oocyte maturation were observed. After 4hr and 24hr culture with or without OCCs, media containing 0.4% BSA, 10% HCS and 10 lU hCG respectively were collected and analyzed for changing concentrations of estradiol (E2), progesterone(P4), testosterone(T), and PGF2. There were no elevation of E2, T, and PGF2 by OCCs culture, but minute elevation of P4 level by 24hr OCCs culture in hCG supplementation (p=0.048). The stimulating pattern of cumulus expansion of OCCs by HCS and hCG supplementation was similar to our previously report using Ham's F-10 media, however oocyte maturation rates after 24hr OCCs culture in all media were increased by 20~30% compared to Ham's F-10 media. These results suggest that LH in HCS induce cumulus expansion probably by P4 secretion of OCCs, and TC199 is efficient media for immature mouse oocyte maturation.
Animals ; Chorionic Gonadotropin ; Cumulus Cells* ; Dinoprost ; Estradiol ; Humans* ; Luteinizing Hormone ; Mice ; Oocytes* ; Serum Albumin, Bovine

Bovine serum albumin (BSA), which is present in bovine plasma, is one of the major allergens affecting patients with food allergies induced by milk and meat. It is also commonly used in research laboratories. Although some reports have documented food allergies associated with BSA, BSA-induced occupational asthma has not been reported. We report a case of occupational asthma and rhinitis in a laboratory worker caused by the inhalation of BSA powder, in which an IgE-mediated response was suggested as the pathogenic mechanism.
Allergens ; Asthma, Occupational ; Food Hypersensitivity ; Humans ; Inhalation ; Meat ; Milk ; Milk Hypersensitivity ; Plasma ; Rhinitis ; Serum Albumin, Bovine

Bovine serum albumin (BSA), which is present in bovine plasma, is one of the major allergens affecting patients with food allergies induced by milk and meat. It is also commonly used in research laboratories. Although some reports have documented food allergies associated with BSA, BSA-induced occupational asthma has not been reported. We report a case of occupational asthma and rhinitis in a laboratory worker caused by the inhalation of BSA powder, in which an IgE-mediated response was suggested as the pathogenic mechanism.
Allergens ; Asthma, Occupational ; Food Hypersensitivity ; Humans ; Inhalation ; Meat ; Milk ; Milk Hypersensitivity ; Plasma ; Rhinitis ; Serum Albumin, Bovine

Cell adhesion to material surface plays an important role in regulating cell function such as proliferation and differentiation. Surface patterning provides a useful method to control cell spatial distribution and adhesion to substance. Here microcontact printing and microfluidic channels were introduced to pattern MC3T3 E1 osteoblasts on silicon substance. Dichlordimethylsilane (DMS) was used in microcontact printing to generate the alternating domains of DMS and non-DMS, and cells preferentially adhered to the non-DMS and hydrophilic region. On the patterned surfaces generated from collagen and albumin solutions with microfluidic channels, cells preferentially localized in the collagen-coated region. The results also showed that micropatterning could be a useful method to study the effect of surface chemistry on cell adhesion and other functions.
Cell Adhesion ; Cells, Cultured ; Collagen ; chemistry ; Dimethylpolysiloxanes ; chemistry ; Osteoblasts ; physiology ; Serum Albumin, Bovine ; chemistry ; Surface Properties

OBJECTIVETo observe the effects of different cell lysis buffers on protein quantification with Bradford method and bicinchoninic acid (BCA) method.

METHODSBradford method and BCA method were used to determine the concentration of bovine serum albumin (BSA) in different solutions (distilled water, cell lysis buffer used in two-dimensional differential in-gel electrophoresis and three kinds of cell lysis buffers used in conventional two dimensional gel electrophoresis), as well as the protein concentrations of cell lysates using these different lysis buffers. Bradford method was also applied to determine the protein concentrations of samples with repeated freeze thaw cycle, in different colorimetric cylinders, or using different standard curves from different periods.

RESULTThe protein measurements increased for 1.2 to 2 fold when different cell lysis buffers were used in Bradford method, but the measurements increased with the increased concentration of BSA (r=0.989 approximately 0.996, P<0.05). For BCA, measurement reading increased about thousands times higher, even overflowed the limits of machine. Protein measurements didn't change significantly, only showed a declined trend after repeated freeze thaw cycle, while no significant changes were found using different colorimetric cylinders or standard curves from different periods.

CONCLUSIONBradford method may be the choice of the protein quantification in proteomics. However, optimization is required for specific experimental conditions.

OBJECTIVETo establish a direct and fast method separating calcium levofolinate and calcium dextrofolinate in a bovine serum albumin stationary phase chiral column.

METHODSUsing EC150/4 RESOLVOSIL BSA-7(150 mm x 4 mm) chiral separation column, with 0.20 mol/L, pH=5.0 phosphate buffer as mobile phase HPLC method was performed to separate calcium folinate enantiomers.

RESULTThe capacity factor and resolution of the two calcium folinate enantiomers were greatly affected by mobile phase buffer concentration,pH and the column temperature. And the retention time of calcium levofolinate and calcium dextrofolinate were 18.5 min and 22.6 min, respectively. The resolution, R(s)=1.49.

CONCLUSIONCalcium folinate enantiomers are separated successfully using this method.