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Results for “SERUM ALBUMIN”

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At least 19 recordsLinked to original sources
PubMed2006

Confocal immunolocalization of bovine serum albumin, serum retinol-binding protein, and interphotoreceptor retinoid-binding protein in bovine retina.

PURPOSE: Recently it has been shown that the transport as well as clearance of retinol from isolated rod photoreceptors requires an extracellular factor. Interphotoreceptor retinoid-binding protein (IRBP) is a component of the interphotoreceptor matrix (IPM) and is known to bind visual cycle retinoids. Serum albumin and serum retinol-binding protein (sRBP), proteins capable of binding retinoids, have also been reported to be components of the IPM. It is of interest to know the components present in the IPM that are capable of binding visual cycle retinoids and that also facilitate rhodopsin regeneration. The purpose of this study was to determine the localization of serum albumin, sRBP, and IRBP in bovine retina using immunofluorescence analysis. METHODS: Fresh bovine eyes, obtained from a local abattoir, were fixed immediately after enucleation. Tissue sections (100 microm) were incubated with primary antibodies to bovine serum albumin (BSA), sRBP, and IRBP. Sections were washed then incubated 4 h with 4'-6-Diamidino-2-phenylindole (DAPI), Alexa Fluor(R) 488 goat antimouse, and Alexa Fluor 568 goat antirabbit secondary antibodies. Sections were analyzed using a laser scanning confocal microscope equipped with Nomarski optics. Western immunoblot analysis of bovine retinal tissues and protein standards was performed using the primary antibodies to BSA, sRBP, and IRBP to show specificity to their respective antigens. RESULTS: Immunoblot analysis showed that monoclonal anti-BSA was highly specific for BSA detecting only a single band at about 67 kDa. Antihuman sRBP and antibovine IRBP were also highly specific, recognizing a single band at about 25 and about 133 kDa, respectively. No immunopositive bands were observed in bovine neural retinal when probed with the anti-sRBP antibody; however, a single immunoreactive band at about 67 and about 133 kDa was detected in bovine neural retina by the anti-BSA and IRBP antibodies, respectively. Immunofluorescence analysis showed labeling for IRBP throughout the IPM. IRBP labeling was especially associated with the outer segments of photoreceptors and also with the apical surface of the retinal pigment epithelium. Immunofluorescence labeling for serum albumin was associated only with the lumen of retinal and choroidal blood vessels. Staining for both serum albumin and sRBP in the IPM was negative. CONCLUSIONS: Immunofluorescence analysis of fresh bovine eyes using antibodies to BSA and sRBP clearly shows that serum albumin and sRBP are not components of bovine IPM. IRBP, on the other hand, is localized to the IPM where it is available for the binding and transport of visual cycle retinoids. From these data we conclude that serum albumin and sRBP are not factors that could participate in the binding as well as transport of visual cycle retinoids in the IPM of bovine retina.

Animals↗
PubMed1983

Serum albumin, serum antiproteases and polymorphonuclear leucocyte neutral collagenolytic protease in the tear fluid of patients with corneal ulcers.

Using a micro-electroimmune assay, the concentration of polymorphonuclear leucocyte neutral collagenolytic protease, serum-albumin, alpha-1-antitrypsin and alpha-2-macroglobulin were measured in the tear fluid from 18 eyes of 16 patients with severe, melting corneal ulcers. By this method, PML-c-ase was the first time detected in tear fluid. All proteins normalized during healing of the ulcer. The findings are indicative of an important role for PML-proteases in the degradation of the corneal stroma, and of a regulative effect of the serum antiproteases leaking into the tear fluid from inflamed conjunctival vessels.

Adolescent↗
PubMed1983

Serum albumin, serum antiproteases and polymorphonuclear leucocyte neutral collagenolytic protease in the tear fluid of normal healthy persons.

Using a micro-electroimmune assay and a 'non-reflex stimulating' method to collect normal tear fluid, the concentration of the serum proteins albumin (S-A), alfa-1-antitrypsin (alpha 1A), alfa-1-antichymotrypsin (alpha 1X) and alfa-2-macroglobulin (alpha 1M) was determined in the tear fluid of 53 normal persons. In addition, the tear fluid was tested for the content of polymorphonuclear leucocyte neutral collagenolytic protease (PML-c-ase). PML-c-ase and alpha 1X could not be detected in any tear samples. The concentrations of S-A, alpha 1A and alpha 1M were constant over time, and showed no variation with sex, age or between the right and left eyes. There was no correlation between the concentration levels of the detected proteins in the tear fluid and correlation between tear fluid levels and corresponding serum concentration levels of the proteins could not be shown.

Adolescent↗
PubMed1984

Binding of [3H]mianserin to bovine serum albumin, human serum albumin and alpha 1-acid glycoprotein.

Scatchard plots which were curvilinear with negative slopes were obtained when the binding of [3H]mianserin to bovine serum albumin (BSA), human serum albumin (HSA), defatted human serum albumin (D-HSA) and alpha 1-acid glycoprotein (alpha 1-AGP) was studied with equilibrium dialysis with constant protein concentrations and various ligand concentrations. Binding parameters were estimated graphically and with a non-linear least-squares computer program, assuming two classes of independent binding sites. alpha 1-AGP had the highest binding affinity (K) and binding capacity (nK). The binding parameters, n and K were not independent of protein concentration when the BSA concentration was varied. Linear atypical Scatchard plots with positive slopes were obtained when the protein concentration was varied for BSA, HSA and D-HSA, at a fixed ligand concentration.

Animals↗
PubMed1999

Chiral discrimination in the transport of ketoprofen and ibuprofen esters through an aqueous phase mediated by various serum albumins.

Serum albumins that act as carriers discriminated between enantiomers of alkyl esters of ketoprofen and ibuprofen in transport in the O/W/O (oil/water/oil) system using a U-shaped cell. The transport rate and the preferred enantiomer of the esters were substantially affected by pH, temperature, and species of albumin. Among five serum albumins studied, bovine serum albumin (BSA) showed the largest rate constant and rat serum albumin (RSA) manifested the highest enantioselectivity. Regarding enantiomer selectivity in transport overall, it is anticipated that the ester uptake step plays an important role for BSA, whereas the ester release is the key step for RSA.

Animals↗
PubMed1968

Stimulation of photoreactions of isolated chloroplasts by serum albumin.

Serum albumin was shown to stimulate markedly various photoreactions in isolated bean and lettuce chloroplasts. The maximal effect was obtained when this compound was present during the homogenization step and continuously in the chloroplast preparation. The "basal" electron transport was enhanced using various acceptors and stimulation was obtained also in the presence of uncouplers. The quantum requirement for ferricyanide reduction was appreciably reduced. Serum albumin increased the rate of cyclic phosphorylation and the ratio of P/e(2) in non-cyclic phosphorylation. The increase in phosphorylation is supposedly due to inhibition of the rate of decay of the high energy non-phosphorylated intermediate, X(E). It is postulated that serum albumin affects chloroplast photoreactions by binding endogenously released unsaturated fatty acids.

Adenosine Triphosphate↗
PubMed1976

Conversions of prostaglandin endoperoxides by glutathione-S-transferases and serum albumins.

Serum albumins of certain animal species (cow, sheep, pig) accelerate the decomposition of prostaglandin endoperoxides, with formation of large amounts of prostaglandin D. The reaction is inhibited by arachidonic acid, which suggests an interaction of the endoperoxide with the fatty acid binding sites of serum albumin. Glutathione-S-transferases, in the presence of glutathione, convert the endoperoxide into a mixture of prostaglandin F2alpha, E2 and D2. The prostaglandin D/E-ratio depends on the transferase used. The known rat liver transferases give mainly prostaglandin F2alpha and E2, but a new transferase in sheep lung was discovered which gives rise to large quantities of prostaglandin F2alpha and D2. The sheep lung transferase was purified to homogeneity. Two iso-enzymes with identical enzymic activity were obtained. The major component (transferase SL 2, an iso-enzyme of glutathione-S-transferase, EC 2.5.1.18) has a molecular weight of 45 000 and consists of two subunits. Its isoelectric point is 9,8-9.9. These properties, as well as the amino acid composition and the substrate specificity for typical transferase substrates, indicate a close resemblance to transferase B (ligandin), a major binding protein of rat liver. Although purified glutathione peroxidase from erythrocytes is very active in catalysing the reduction of the 15-hydroperoxy group of prostaglandins, it does not have any effect on the decomposition of the endoperoxide group.

Animals↗
PubMed1982

The lanthanide-induced N = to F transition and acid expansion of serum albumin.

Serum albumin exists in the native or N conformation between pH 5 and 7. As the pH is lowered from 5 to 3.5, the protein undergoes a conformational change resulting in expansion, known as the N = to F (partially acid expanded) transition. As the pH is lowered still further to 2, the protein continues to expand. In the present study, using the techniques of circular dichroism, fluorescence, and UV difference spectroscopy, lanthanide ions at concentrations between 1-30 mM have been shown to produce both changes in the albumin structure analogous to the N = to F transition and acid expansion of bovine serum albumin at a constant pH near 6.

Cations↗
PubMed2002

Simple and sensitive high-performance liquid chromatographic method for the investigation of dynamic changes in the redox state of rat serum albumin.

Serum albumin is a mixture of mercaptalbumin (reduced form) and non-mercaptalbumin (oxidized form), i.e. a protein redox couple in serum. To investigate dynamic changes in the redox state of rat serum albumin (RSA), we developed a simple and sensitive high-performance liquid chromatographic (HPLC) system using an ion-exchange column with a linear gradient of ethanol concentration. Furthermore, we applied this HPLC system to examine dynamic changes in the redox state of RSA caused by severe oxidative stress such as exhaustive physical exercise. Using this system, we successfully separated RSA to rat mercaptalbumin (MA(r)) and rat non-mercaptalbumin (NA(r)), and also found the best conditions for the clear separation of RSA. In the experiments with exhaustive exercise, mean values for the MA(r) fraction in control and exercise groups were 76.2+/-1.8 and 69.0+/-3.5%, respectively. The MA(r) in the exercise group was significantly oxidized compared with that of the control group (P<0.01). These results suggested that RSA might act as one of the major scavengers in extracellular fluids under severe oxidative stress.

Animals↗
PubMed2003

Biological role of adduct formation of the ruthenium(III) complex NAMI-A with serum albumin and serum transferrin.

NAMI-A is an innovative ruthenium(III) complex with a very encouraging preclinical profile of metastasis inhibition, which is undergoing initial phases of clinical trials. To assess the pharmacological relevance of the drug fraction associated to plasma proteins, adducts of NAMI-A with either serum albumin or serum transferrin were prepared and their biological effects tested in vitro and in vivo. Specifically, adducts of NAMI-A with either serum albumin or serum transferrin, prepared and characterized at a ruthenium-to-protein molar ratio of 4:1, were evaluated in vitro on the KB human tumor cell line and in vivo on the MCa mammary carcinoma tumor. The effects of NAMI-A/protein adducts on cell viability and on cell cycle progression were found to be far smaller than those produced by free NAMI-A. GFAAS measurements point out that the amount of ruthenium that gets into cells is drastically reduced when NAMI-A is presented in its protein-bound form. In vivo use of NAMI-A adducts with albumin and transferrin resulted markedly less effective on lung metastasis reduction, than free NAMI-A. Overall, the present results suggest that binding to plasma proteins causes a drastic decrease of NAMI-A bioavailability and a subsequent reduction of its biological activity, implying that association to plasma proteins essentially represents a mechanism of drug inactivation.

Animals↗
PubMed2004

Bone mineral density, serum albumin and serum magnesium.

OBJECTIVES: This study explores clinical and laboratory abnormalities that contribute to the prevalence of bone fractures in frail and control elderly patients, to ascertain factors that relate to bone strength and fragility. METHODS: Patients were selected as free from renal failure and not taking supplements or medications that affect their magnesium status, and categorized according to their underlying diseases, sex and age, and evaluated by tests of bone strength. RESULTS: Findings, differentiating elderly patients on the basis of their magnesium, calcium, serum albumin, body mass, bone mineral density and their fracture occurrence were tabulated. CONCLUSION: Evidence is presented of low magnesium and albumin serum levels, especially in women with low bone density, as well as of low calcium and trace minerals.

Aged↗
PubMed2006

Prognostic value of serum albumin combined with serum C-reactive protein levels in older hospitalized patients: continuing importance of serum albumin.

BACKGROUND AND AIMS: Although both serum albumin and C-reactive protein (CRP) levels are separately recognized as predictors of adverse outcomes in many illnesses, the predictive value of their combination for adverse outcomes has not been evaluated. We therefore sought to examine the prognostic value of serum albumin for in-hospital mortality in the presence or absence of severe inflammation, as indicated by high CRP levels. METHODS: In this cohort study, we measured serum albumin and CRP levels in 1638 older patients (aged 65 years or older) hospitalized for medical problems, and examined their utility, both separately and in combination, for predicting in-hospital mortality. RESULTS: In separate analyses of CRP and albumin, both high CRP levels (> or =5 mg/dl) and hypoalbuminemia (<3.5 g/dl) were associated with risk of in-hospital death. After dividing participants into four groups based on CRP and albumin levels (<5 mg/dl CRP and <3.5 mg/dl albumin), subjects with severe inflammation (CRP > or =5 mg/dl) and hypoalbuminemia were associated with an adjusted relative risk (ARR) of 3.8 for in-hospital mortality when compared with the reference (high albumin and low CRP). Even in the absence of severe inflammation, the presence of severe hypoalbuminemia was associated with an ARR of 2.6 for in-hospital mortality, when compared with patients without hypoalbuminemia. CONCLUSIONS: Both serum CRP and albumin levels are predictors of in-hospital mortality. However, high serum albumin levels may have a protective effect in older patients, regardless of degree of inflammation. Serum albumin levels remain a useful predictor for in-hospital mortality in older hospitalized patients.

Acute Disease↗