Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0393754 (HSA)
 2,996 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Studies were undertaken to determine whether BSA immobilized in collodion membranes adherent to activated charcoal particles, would be capable of specifically removing circulating BSA antibody in vitro and in vivo in an extracorporeal system in dogs. Up to 59-8 mg of BSA were retained in collodion membranes adherent to small particles. In vitro studies demonstrated that immobilized BSA could specifically reduce BSA binding activity from circulating antisera. For in vivo studies, an extracorporeal circulation system was established and arterial blood was circualted through a continuous flow celltrifuge in which plasma was separated from formed elements of the blood. Only plasma was circulated over the BSA collodion-charcoal immunoadsorbent. Anti-BSA and anti-HSA atibodies were passively infused into dogs and, after an equlibration period of 12 or 15 min, plasma was passed over the BSA collodion-charcoal immunoadsorben. Plasma exhibited a sharp reduction in BSA binding over the next 30-60 min with only slight reduction in anti-HSA binding the same period. Dogs, actively immunized to BSA and HSA, were also treated by extracorporeal plasma perfusion over BSA collodion-charcoal. A specific decline in BSA binding of sera, was again observed with minimal changes in HSA binding. A post-perfusion rebound of BSA binding was observed which reached pre-perfusion levels after 6-8 days. A second treatment during the rebound period also resulted in a specific decline in BSA binding with a similar pattern of antibody rebound. There were no significant changes in I-labelled BSA recorded on the charcoal before and after in vivo procedures and no signifcant alterations in haematocrit, serum sodium, potassium, calcium, magnesium or creatinine levels before and after the procedures. These data suggests that antigen-coated charcoal may specifically withdraw circulating antibodies in vivo with minimal release of the entrapped antigen and little alteration in the host's haematological and biochemical status.
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PMID:Specific removal of antibody by extracorporeal circulation over antigen immobilized in collodion-charcoal. 86 46

The efficacy of antiviral drugs and vaccines administered intranasally may depend upon the technique of application. The distribution and time-course of removal of human serum albumin-technetium 99m (HSA-Tc 99m)-instilled intranasally were studied in eleven healthy volunteers using a gamma camera and an anterior sodium iodide scintillation detector. In 100 randomized studies material was delivered as drops in the supine position or as a spray to seated subjects. A significantly higher proportion of 'good' distributions (62 in 73 tests) was obtained with drops compared with spray (1 in 27). The volume administered was varied between 0.10 ml and 0.75 ml and the concentration of HSA was changed from 3 to 30% with no significant effect upon the distribution of time-course of removal; pertechnetate in isotonic saline was distributed and removed in a manner comparable to HSA-Tc 99m. Activity recorded by the detector showed an initial rapid fall associated with removal of most of the material from the nasal cavity, followed by a slower decline associated with the removal of material mainly from the anterior region of the nose. A multidose study confirmed that frequent administration by drops is required to maintain a high level of activity in the nasal cavity. Using this technique it should be possible to correlate measurements of antiviral efficacy and vaccines take-rates with certain characteristics of intranasal applicators; such studies may lead to the design of better devices.
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PMID:Distribution and removal of human serum albumin-technetium 99m instilled intranasally. 97 82

Mercaptoundecahydrododecaborate (BSH) is an important agent in boron neutron capture therapy (BNCT) of various cancers. A simple and rapid analytical method for the measurement of mercaptoundecahydrododecaborate in aqueous solution and in urine by Fourier transform infrared spectroscopy has been developed. A thin-pathlength sampling apparatus was used to minimize the strong absorption of water. The subtraction of water absorbance from sample spectra resolved a B-H band at 2493 cm-1. The quantitative measurement of BSH concentration was carried out by integrating the B-H band above baseline in the range of 2534-2440 cm-1. The lower limit of measuring the concentration of sodium BSH (Na2B12H11SH) in our experiment was 10 micrograms/ml (about 5 ppm of boron). This method measures the hydroborate (B-H) concentration instead of total boron and, thus, may be utilized to measure the BSH concentration in in vivo samples for metabolic studies.
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PMID:Quantitative analysis of mercaptoundecahydrododecaborate by Fourier transform infrared spectroscopy. 140 4

We measured the binding of a drug oxyphenylbutazone to the N-terminal peptic fragment of human serum albumin in 0.1 M Tris buffer, pH 8.0 (Kass = 2.4 10(5) M-1) and in reverse micelles of sodium bis(2-ethylhexyl) sulfosuccinate and buffer in isooctane (Kass. = 2.7 10(5) M-1). In the absence of any measured change in conformation of the fragment in reverse micelles, the peptide affinity for the drug is not decreased, in contrast to what is observed in intact albumin (HSA) under similar conditions. The interaction and the subsequent unfolding of HSA at the membrane-mimetic interface, constitutes thus a drug release-facilitating mechanism.
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PMID:A drug release-facilitating mechanism for human serum albumin in reverse micelles: requirement of a structural switch. 155 38

Kinetics of boron disposition after single intravenous injections of two different doses (25 and 50 mg/kg) of mercaptoundecahydrododecaborate sodium (Na2B12H11SH; BSH) was studied in rabbits. Residual boron concentrations in various organs and tissues (heart, lungs, liver, spleen, kidney, adrenals, and brain) were also determined after seven daily injections of the same doses of BSH. Boron blood and tissue concentrations were measured by atomic emission spectrometry. In the majority of animals, the decline of boron blood concentrations after a single intravenous injection of either dose was biphasic, being consistent with a two-compartment model of boron disposition in the body. Although mean boron blood concentrations were roughly proportional to the BSH dose delivered, the mean total body clearance of boron from the body was 3 times lower (6.5 +/- 1.9 ml min-1 kg-1) after a dose of 50 mg/kg than after the injection of 25 mg/kg (22.4 +/- 7.9 ml min-1 kg-1), the difference between the means being statistically significant (P less than 0.05). Moreover, the mean terminal half-life of boron in blood was prolonged after the injection of 50 mg/kg (14.5 +/- 5.5 h) as compared with that found after the 25-mg/kg dose (3.5 +/- 0.9 h). On the other hand, the different BSH doses did not result in marked differences in the mean values obtained for the volume parameters - the volume of the central compartment (1.3 +/- 0.4 vs 1.3 +/- 0.5 l kg-1) and the volume of distribution at steady state (4.7 +/- 1.3 vs 6.0 +/- 4.0 l kg-1) - both of which were high, indicating extensive binding of the compound not only in the blood but also in tissues. Residual concentrations of boron found after seven daily injections of both doses of BSH were highest in the kidneys, the difference in the mean values being relatively small (33.6 +/- 6.1 vs 39.0 +/- 10.7 micrograms/g tissue). In the majority of other organs (heart, lung, liver, spleen, brain, adrenals), the residual concentrations after a dose of 50 mg/kg were disproportionately higher than those measured after the injection of 25 mg/kg, and the mean values corresponded to the reduced total body clearance rather than to the increased BSH dose. The saturability of BSH binding to blood and tissue proteins is suggested as a possible explanation for the dose dependency of the total clearance of boron from the body and the accumulation of BSH in organs and tissues.
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PMID:Dose-dependent disposition kinetics and tissue accumulation of boron after intravenous injections of sodium mercaptoundecahydrododecaborate in rabbits. 156 87

The following boron-containing nucleoside and glucose derivatives have been synthesized as potential boron delivery agents for boron neutron capture therapy (BNCT): 2'-O-(o-carboran-1-ylmethyl)uridine (4a), 3'-O-(o-carboran-1-ylmethyl)uridine (4b), sodium 7-(uridin-2'-ylmethyl)dodecahydro-7,8-dicarba-++ +nido-undecaborate (5), 5'-O-(o-carboran-1-ylmethyl)uridine (9), and 3'-O-(o-carboran-1-ylmethyl)-D-glucose (13). In vitro cellular uptake studies were performed with F98 rat glioma cells. Following 16 h incubation, cellular boron concentrations were determined by direct current plasma atomic emission spectroscopy (DCP-AES). Boron concentrations ranged from 65 to 103 micrograms/g of cells for the neutral closo structures compared with 1.5 micrograms/g of cells for the charged nido species. Cellular uptake of sodium mercaptoundecahydro-closo-dodecaborate (BSH), the compound currently being used in Japan for the treatment of malignant brain tumors by BNCT, was 2 micrograms/g of cells.
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PMID:Synthesis and in vitro evaluation of boronated uridine and glucose derivatives for boron neutron capture therapy. 157 91

A three-dimensional projection reconstruction technique is described for imaging boron-11 distributions, with potential application to boron neutron capture therapy. The method samples a spherical volume of k space uniformly to obtain a 32 x 32 x 32 matrix with voxel size of 0.42 cm3. A signal-to-noise ratio (S/N) of 3 was obtained in 8.5 minutes in a phantom containing 75 micrograms/mL of boron in borocaptate sodium (BSH). Images were obtained in a dog after cessation of an intravenous infusion of BSH and again 30 minutes later, with a maximum boron S/N of about 12. Boron levels in the brain dropped about 6%-8% and were more diffusely distributed on the images obtained 30 minutes after BSH infusion.
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PMID:Boron-11 imaging with a three-dimensional reconstruction method. 162 80

The luminol-enhanced chemiluminescence of zymosan-stimulated polymorphonuclear leukocytes is continuously diminished in the presence of increasing amounts of human serum albumin (from 1 to 30 mg/ml). HSA competes with luminol for hypochlorite as shown by adding sodium hypochlorite to luminol solutions containing HSA. Titration of HSA with NaOCl affects firstly the sulfhydryl and probably the thioether groups and then the amino groups. Coincubation of zymosan-stimulated polymorphonuclear leukocytes and HSA at a ratio corresponding to normal values of healthy men causes a continuous oxidation of sulphur containing functional groups in HSA.
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PMID:On the action of hypochlorite on human serum albumin. 196 76

The aim of this study was to clarify the relationship between the extent of activation of synthetic granula and fibrous carbons and the adsorption of bilirubin from protein solutions. The total pore volumes of granular carbons START, SCN and fibrous activated carbons ACFM were 0.9-2.2. cm3/g and 0.8-1.5 cm3/g, respectively. A parallel increase in volume and specific surface area of micropores lead to a 4-5-fold increase of bilirubin adsorption from a 3% HSA solution. About 3 mg of bilirubin per 1 ml of the working column volume is removed from the solution with a 18 mg/100 ml concentration, after 8 min contact with an adsorbent after 4 hours of perfusion. Removal of bilirubin from model solutions means the conformation of albumin molecules can be restored. Carbon adsorbents synthesized for the elimination of bilirubin from protein-containing solutions can also be called deliganding adsorbents, since under some experimental conditions they eliminate other protein-bound ligands, viz. phenols by 97-99%, bile acids by 90-92% and sodium caprylate by 89-95%.
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PMID:High-porosity activated carbons for bilirubin removal. 204 94

The affinity matrix prepared by the attachment of L-thyroxine (T4) to epichlorohydrine-activated Sepharose 4B biospecifically absorbs the T4-binding globulin (TBG), 25K and 80/27K proteins, immunoglobulin G (IgG) and albumin (HSA) from human normal and retroplacental sera. The absorbed protein patterns were shown to depend on the immobilized T4 concentration, pH, temperature and incubation time. The potent eluents desorbing 85-100% of the protein are 1 mM NaOH, 3 M NH4SCN, 10(-5) M T4 or 3 mM 8-anilinonaphthalene-1-sulfonic acid (ANS) for TBG; NaOH, NH4SCN, 3 mM MgCl2 or 12mM sodium cholate for 25K protein and HSA; NaOH, NH4SCN or MgCl2 for the 80/27K and 25K proteins and IgG. Moreover, T4 desorbs small amounts (6-8%) of the 80/27K and 25K proteins, while sodium cholate elutes about 6% of TBG. The eluted from T4-Sepharose 4B and further purified TBG, 25K and 80/27K proteins display different [125I]T4-binding activities within the pH range from 2 to 9 and differ by their resistance to thermal inactivation at 50-80 degrees C. Double radial immunodiffusion analysis with the use of antisera to TBG, 25K, 80/27K, HSA and IgG demonstrated that the proteins share no common antigenic determinants. It was concluded that the novel 25K and 80/27K proteins represent endogenous components of the human blood thyroid hormone-binding protein system rather than fragments or aggregates of the known T4-binding proteins.
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PMID:[Affinity chromatography of thyroxine-binding proteins from human serum]. 211 Nov 82


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