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)

A RAST has been developed for the measurement of IgE antibodies specific to platinum chloride complexes in sensitized workers. Human serum albumin covalently linked to Sepharose beads by the cyanogen bromide method was reacted with ammonium tetrachloroplatinite (II) (NH4)2PtCl4. This conjugate was more suitable for the RAST, than conjugates of HSA and the platinum salt prepared in solution and then linked to the activated Sepharose, showing better sensitivity and giving lower levels of non-specific uptake of IgE from sera of non-exposed subjects with high total levels of IgE, e.g. allergic bronchopulmonary aspergillotics.
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PMID:Specific IgE antibodies to platinum salts in sensitized workers. 8 84

ELISA was applied for analysis of the HSA-human IgG autoantibody system responsible for the immunoelectrophoretic 'Tailing Albumin' (TA) phenomenon induced in most of the TA patients by prolonged nitrofurantoin therapy. Both hyperimmune porcine anti-HSA and autoimmune human anti-HSA antibodies of the IgG class were detectable by ELISA. The presence of autologous or added HSA had some inhibitory effect upon the detectability of the anti-HSA antibodies. Partial elimination of the autologous HSA by sucrose gradient ultracentrifugation or salt precipitation increased or unmasked the anti-HSA activity of some TA sera. The sensitivity of the ELISA as detector of the anti-HSA autoantibodies of whole human sera was roughly equal to that of the immunoelectrophoretic TA phenomenon. The analogy of the anti-HSA autoantibodies and the rheumatoid factors and the theoretical interest of both of them is stressed.
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PMID:IgG autoantibody to human serum albumin studied by the ELISA-technique. 35 95

Inhalational exposure to trimellitic anhydride (TMA) produces an immediate-type asthmatic or a late respiratory systemic syndrome in certain workers after a latent period of work exposure. TMA has been found to react with proteins to produce a hapten-protein complex (trimellitate [TM] protein) or become hydrolyzed in aqueous, alkaline solutions to produce a salt, NaTM. Using a solid-phase radioimmunoassay technique, antibodies of different Ig classes were detected against TM-protein conjugates. IgE antibody was detected in three of five workers with asthma. IgG and IgA antibodies were detected in most exposed workers but higher levels of antibody were found in symptomatic workers even after long periods without direct TMA exposure. IgM antibody activity against TM-human serum albumin (TM-HSA) was detected but did not differentiate symptomatic from asymptomatic workers. NaTM served as a hapten for study because it does not react with proteins to form a hapten-protein complex as TMA does. The NaTM only partially inhibited IgG antibody activity against TM-HSA and much smaller amounts of TM-HSA than of NaTM were required to neutralize IgG antibody. A similar result was found with TM-ovalbumin. The latter results suggest that some IgG antibody is directed against a TM-protein moiety, probably a TM-amino acid determinant. In contrast to IgG, marked inhibition by NaTM of IgA and IgM antibody against TM-HSA was found in the sera studied.
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PMID:Human antihapten antibodies in trimellitic anhydride inhalation reactions. Immunoglobulin classes of anti-trimellitic anhydride antibodies and hapten inhibition studies. 71 61

Levonorgestrel (LN), 3-Keto-desogestrel (KDG), norethisterone (NET), and gestodene (GST) were investigated in the recirculating rat liver perfusion model. Progestins were dissolved in buffered salt solution (MI), BSA containing (MII) or HSA and sex hormone binding globulin (SHBG) containing medium (MIII) at a concentration of about 60 ng/ml. Each 3-5 female rat livers were perfused with MI, MII, and MIII for 1 h. Perfusion medium, liver biopsies and total bile were analyzed for progestin levels by specific radioimmunoassays. Protein binding characteristics were determined in media and tissue. In all experiments bile (remaining liver) contained less than 1% (3%) of respective progestin dose demonstrating an almost complete biotransformation of all drugs by rat livers, irrespective of used medium. With MI, metabolic clearance rates (MCRs) and half-lives (t1/2) were not different for the four progestins. With MII, the actual progestin levels were generally higher than with MI, but half-lives were not changed. MCRs were close to the perfusion rate at the start of experiments but decreased to about 50%. MCRs of free and total drug levels were identical. Protein binding of 70-80% did not change with time. With MIII, the half-lives increased 1.5 fold (NET), 2.8 fold (KDG), 3.1 fold (GST) and 3.2 fold (LN) and MCRs accounted for 50-70% of perfusion rate at the beginning. The time courses of further MCR decreases were different for the various progestins and can be attributed to differences in specific binding of drugs to SHBG. Clearly, the presence of SHBG in MIII induced a shift of drug from liver tissue into the perfusion medium.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Influence of protein binding on the metabolic clearance rate of synthetic progestins in the rat liver perfusion model. 144 81

Two platinum (Pt) refinery workers with work related asthma was reported. The serum specific IgE and skin test for Pt antigen were positive. Ten guinea pigs were immunized with Pt-BSA conjugates employing CFA or AHG adjuvant via intraperitoneal. After 5-8 weeks, 33.3% of the sensitized animals experienced asthma attacks after a Pt-HSA challenge. The dynamic ventilation pulmonary imaging with 99mTc-DTPA showed a central accumulation of radioactivity. A specific IgE and IgG type antibodies were developed in 66.7% of sensitized animals by PCA test. Results of these suggested that platinum complex salt have antigenic specify. Allergic response play an important role in the mechanism of Pt induced asthma.
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PMID:[A study on the immunology and etiology of platinum induced asthma]. 181 74

The specificity of the p15 proteinase of myeloblastosis-associated virus (MAV) was tested with nonviral high molecular weight substrates and with synthetic peptides. Peptides with sequences spanning known cleavage sites in viral polyproteins of Rous sarcoma virus (RSV) and avian leukemia viruses, as well as in BSA and HSA, were synthesized, and the rate of their cleavage by the MAV proteinase was compared. Synthetic peptides require for successful cleavage at least 4 residues at the N-terminal side and 3 residues at the C-terminal side. The proteinase shows a preference for hydrophobic residues with bulky side chains (Met, Tyr, Phe) in P3, although Arg and Gln can also be accepted. Small hydrophobic residues are required in P2 and P2', and large hydrophobic residues (Tyr, Met, Phe/p-nitro-Phe) are preferred in both P1 and P1'. The difference between the specificity of the p15 proteinase and that of the HIV-1 proteinase mostly pertains to position P2' of the substrate, where bulkier side chains are accepted by the HIV-1 proteinase (Richards et al., 1990). A good chromogenic substrate for the MAV and RSV proteinases was developed and used to further characterize the MAV proteinase activity with respect to ionic strength and pH. The activity of the proteinase is strongly dependent on ionic strength and pH. Both the kcat and Km values contribute to a higher cleavage efficiency at higher salt concentrations and show a bell-shaped pH dependence curve with a sharp maximum at pH 5.5 (kcat) and 6.5 (Km).
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PMID:Specificity studies on retroviral proteinase from myeloblastosis-associated virus. 184 25

This study was performed to provide information on the determinants of lymph flow by comparing the effect of venous stasis and hypoproteinaemia in the rat tail. This low-compliant tissue was chosen in an attempt to induce preferential changes in interstitial pressure or volume. The removal rate (kAlb) of 125I-labelled human serum albumin (I-HSA) injected subcutaneously was monitored with external gamma-counting equipment and used as a measure of lymph flow. Interstitial fluid hydrostatic pressure (Pi) was measured with wick-in-needle technique, and interstitial fluid was collected post mortem by dry wicks. Colloid osmotic pressure of plasma (COPp) and wick fluid (COPi) was measured with a colloid osmometer. In a separate group of experiments, 51Cr-EDTA and [125I]HSA were used to measure the interstitial fluid volume. Venous stasis, induced by bilateral ligation of the external tail veins, increased interstitial fluid hydrostatic pressure from 1.7 to 16 mmHg and kAlb from 0.030 to 0.063 h-1, whereas tail circumference was nearly constant. Interstitial volume averaged 1.17 ml/g dry weight in control animals and 1.27 ml/g during increased venous pressure. Daily injections of aminonucleoside in salt-loaded rats (0.3% NaCl as drinking water) reduced colloid osmotic pressure of plasma from 19.1 to 8.5 mmHg and of wick fluid from 11.2 to 2.9 mmHg, while interstitial fluid hydrostatic pressure increased to 5.2 mmHg. The removal rate of 125I-labelled human serum albumin increased to 0.113 h-1, compared to 0.051 h-1 in salt-loaded controls. The interstitial volume showed a marked increase in salt-loaded hypoproteinaemic rats, 1.75 ml/g dry weight, compared to 1.30 ml/g in salt-loaded controls.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effect of longstanding venous stasis and hypoproteinaemia on lymph flow in the rat tail. 187 57

HBsAg is known to bind to human serum albumin polymerized by glutaraldehyde, human serum albumin has been found in preparations of HBsAg by several investigators. However, it is not yet known whether natural human serum albumin binds to hepatitis B virus under physiological conditions. We studied the binding between natural or recombinant HBsAg and monomeric human serum albumin by immunological, biochemical and biophysical methods. The binding capacity of 20-nm HBs spheres was variable but ranged up to six molecules HSA/sphere. A reversible binding site for human serum albumin was exclusively localized in the preS2 domain, whereas the S domain was inactive in vitro. Human serum albumin copurified with HBsAg of human origin during gel chromatography or sucrose-gradient centrifugation. This human serum albumin was monomeric in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The preS2-bound part of the human serum albumin could be removed from HBsAg by high-salt, such as CsCl centrifugation, but another part could only be removed by treatment with a disulfide cleaving reagent. Most of this covalently bound human serum albumin was retained at the HBsAg particle after complete cleavage of medium-sized HBs protein with trypsin. This indicates a second way in which albumin binds irreversible to cysteine(s) of the small HBs protein (SHBs, P24 and GP27).
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PMID:Interaction between hepatitis B surface proteins and monomeric human serum albumin. 216 67

Penicillin G (PNG) has been demonstrated to elicit T-cell responsiveness in vitro in allergic patients by means of a lymphocyte transformation test (LTT). As it was not clear how, or in what form, the stimulatory PNG determinants were inducing cellular proliferation, we compared the immune response elicited by different PNG preparations. Peripheral blood lymphocytes (PBL) of patients with proven PNG allergy were isolated, and proliferative responsiveness to soluble PNG alone, soluble PNG-protein conjugates (BPO-HSA, BPO-PL, BPO-HEX), and non-reactive penicilloate salts, was evaluated. An autologous mixed lymphocyte culture (MLC) using penicilloylated stimulator cells, was used to test responsiveness to membrane-bound PNG. We found that the addition of either 1000 micrograms/ml of potentially-reactive PNG to cell cultures, or of penicilloylated autologous cells was stimulatory, whereas non-reactive PNG salt, and soluble PNG conjugates were not stimulatory. Considering current and earlier findings, it appears that T cell immunity in these patients is directed towards PNG-modified "self", as PNG-modified autologous cells are potent stimulators in PNG-allergic individuals.
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PMID:Penicillin-allergic patients react to penicillin-modified "self". 252 72

Nuclear proteins contain specific regions that are required for entry into the nucleus. Using ligand blotting, we have shown that a 67-kDa yeast nuclear envelope protein (p67) recognizes synthetic peptides containing the yeast histone H2B or simian virus 40 large tumor antigen nuclear localization sequence. Both free peptide and peptide conjugated to human serum albumin are recognized. The interaction between p67 and the nuclear localization sequences is specific; neither a mutant peptide that is incompetent for nuclear transport in vivo nor HSA can interact with p67 on blots. Moreover, although the wild-type peptide competes for binding to p67, the mutant peptides do not. p67 appears to be located at the nuclear envelope and is not present in other subcellular fractions. The nuclear localization sequence-binding protein is not extracted from the nuclear envelope with nonionic detergents and only partially extracted with high-salt buffer or 8 M urea, suggestive of a tight association with the nuclear envelope. Together our results are consistent with a role for p67 in nuclear transport.
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PMID:Identification and characterization of a nuclear localization sequence-binding protein in yeast. 268 60


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