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)

All 306 South African platinum refinery workers (116 white, 190 coloured) accepted for employment on grounds of absence of evidence of atopy were investigated using the skin prick test and RAST to detect sensitivity to platinum, palladium, and rhodium salts. RAST studies were made for these, together with HSA and DNP-HSA RAST. Of the 306 workers, 38 had a positive skin prick test to the platinum halide salts; of these, one gave a positive reaction to the palladium salt and six to the rhodium salt. There were no isolated positives to the rhodium and palladium halide salts. Total IgE levels were raised in 24 of the 38 (63%) platinum salt prick test positive workers compared with only 43 of the 268 (16%) prick test negative group (p less than 0.001). Positive RASTs were obtained in 62% of those with positive skin tests to the platinum salts. Four of the six giving positive rhodium salt skin tests gave a positive RAST to rhodium salt. Of these, two gave positive RASTS to HSA and all four to DNP-HSA. The palladium salt RAST was negative in the single skin test reactor. In the platinum salt skin test positive group a raised HSA RAST was obtained in 10.5% compared with only 2.5% in the skin negative group. Twenty one per cent of the platinum salt skin positive group had a raised RAST score to DNP-HSA with only 3.5% (4/116) in the skin test negative group, of whom three also had a raised HSA RAST. The latter findings are suggestive of IgE antibody production to new antigenic determinants in HSA produced by conjugation with the platinum salts.
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PMID:IgE antibody responses to platinum group metals: a large scale refinery survey. 293 74

Human alpha-fetoprotein (AFP) and serum albumin (HSA) were studied by hydrophobic interaction chromatography. A close resemblance was observed both in the native state and after various perturbations (pH, salt and alcohol) indicating a significant similarity in their molecular structures. Both proteins displayed similar hydrophobic properties which apparently were different from those of other globular proteins. In agreement with the domain structure proposed by Brown (1976), our results indicated that surface nonpolar side chains of both the native HSA and AFP produced large hydrophobic areas located solely in crevices.
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PMID:Similarity of hydrophobic properties of alpha-fetoprotein and albumin. 617 69

Previous studies of the serum binding of the photosensitizer hematoporphyrin (Hp) have given widely different results. The serum binding of Hp is therefore further illuminated by experiment and discussion. Ultracentrifugal separation of serum is improved and applied to study the binding of Hp to human serum and HSA. The observed distribution of Hp among the serum proteins is compared with the distribution expected from available association constants for Hp binding with individual proteins. The lipoprotein classes and the two major high density proteins (HDP), albumin and gamma-globulin, were separated in a NaCl-KBr gradient by single spin ultracentrifugation (SW 40; 30,000 rpm). HSA- and HDP-bound Hp were similarly distributed in the centrifuged gradient. Centrifugation of Hp-doped HSA separated the unbound Hp (75%) and the HSA-bound Hp (25%). The present association constant for the Hp-HSA complex (10(3)/M) was much lower than earlier published ones (10(6)/M) found by other techniques. The association of Hp with HDP in serum was much stronger than the association of Hp with the isolated HSA (electrophoretic grade). The estimated ratio of HSA-bound to LDL-bound HP in serum was at least 25 times larger than the experimental value. The percentage of LDL-bound Hp decreased with increasing Hp concentration. The serum binding of Hp is the same as that found previously using another rotor and another salt gradient (70.1 Ti, 70,000 rpm, NaCl-CsCl). LDL has high-affinity-low-capacity binding sites for Hp. HSA is the major HDP protein that binds Hp in human serum. The strength of the HSA-Hp complex may depend on the batch of HSA used and upon the absence/presence of other proteins. Proteins may interact in serum in manners that affect the binding of certain drugs. Neither the type of gradient salt nor the field of gravity affected the serum binding of Hp.
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PMID:Separation of lipoproteins, albumin and gamma-globulin by single-step ultracentrifugation of human serum. Application. I: Binding of hematoporphyrin to human serum and to albumin. 754 Apr 98

The binding of keto- and hydroxy bile salts to human serum albumin, the identity of the bile salts binding sites and the identification of the amino acids present in these sites were studied. The keto bile salts cholanate-3-one (C3), cholanate-3,6-dione (C3-6) and cholanate-3-hydroxy-6-one (KHC) were found to quench the native fluorescence emission of albumin. This suggested that the tryptophan residue of human albumin (residue 214) is accessible to the keto bile salts and not to the hydroxy parent compounds. The binding of the keto bile salts was characterized by a simple population of binding sites with Ka ranging from 22 x 10(4) M-1 for the mono keto bile salt (C3) down to 4 x 10(4) M-1 for the hydroxy-keto bile salt (KHC). The substitution of an oxo group at carbon C3 in C3-6 molecule for a hydroxy group (KHC) produce a significant decreasing of the interaction, suggesting that the hybridization state of the carbon at C3 in the steroid ring of the bile salt molecule is also an essential requirement for bile salts binding. It was found that bile salts are bound to the benzodiazepine binding site on human albumin (site II), producing a perturbation on site I, fatty acids and bilirubin binding site. The presence of only one substituent at C3 (oxo or OH) produce an important perturbation on the fatty acid binding sites, decreasing the polarity of the its microenvironment, while a little effect was observed for the dihydroxy and di-oxo-substituted BS, suggesting that the hydroxy substituents at C6, C7 and C12 do not interact in a significant manner with the fatty acid binding sites on HSA. The participation of specific amino acids in albumin-bile salt binding sites depends on the polar groups on the bile salt molecules as exemplified by the quantitatively different role of lysyl residues like those interacting with KHC, C3 and C3-6, and tyrosyl residue interacting with KHC. The following amino acids in human albumin were found to play a role in the bile salts-albumin interaction: lysyl 195 and 225, several arginyls, histidyl 146 and tyrosyl 411.
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PMID:Structural features of the hydroxy- and keto-disubstituted bile salts: human serum albumin binding. 754 67

Staphylococcal neutral phosphatase (NPtase) was purified from two Staphylococcus aureus strains by sequential high salt extraction, ultracentrifugation and ion exchange chromatography. The enzyme showed maximum phosphatase activity at neutral pH, appeared as two bands in SDS-PAGE (31 and 32 kDa), and the isoelectric point was > 10. No close similarity between NPtase and other known bacterial proteins in respect of their N-terminal amino acid sequences was found. Purified NPtase bound rat and human polyclonal IgG [intact and F(ab')2 fragments], IgM, IgA, intact myeloma immunoglobulins, myeloma light chains, gamma heavy chain and, with a much lower affinity, Fc fragments. Furthermore, NPtase can bind serum albumin. Heparin, a highly negatively charged molecule, significantly inhibited NPtase binding to immunoglobulins and HSA, but did not inhibit the binding of specific antibodies to NPtase; this indicates that charge interactions are important. The newly characterized staphylococcal phosphatase with binding properties for immunoglobulin is an interesting bacterial protein that could be involved in post-infectious sequelae.
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PMID:Staphylococcal neutral phosphatase. A highly cationic molecule with binding properties for immunoglobulin. 788 57

Effective thermodynamic parameters of activation of label transition between two microsurroundings in water-protein matrix (WPM) of spin-labelled molecules of serum albumin (HSA-SL) in 0.001 M phosphate buffer, pH 7.3 within concentration range of NaCl (m3) (10(-3) M to 2 M and concentration range of protein (m2) 50 to 200 mg/ml were determined. The phase transition (PT) between two structures of water in WPM is revealed within the m3 range 0.01 M to 0.1 M. It is close to the type I PT and more expressed at high protein concentrations. As m3 increases (to 0.2 M when m2 = 50 mg/ml and to 0.7 when m2 = 200 mg/ml) PT-I is transformed into PT of the critical type. This is indicated to zero values of the higher order derivatives of Gibbs energy of activation with respect to salt concentration, as well as by the maximum values of positive disjoining pressure in these points. The biological significance of this phenomenon is discussed.
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PMID:[Salt-induced critical type phase transition in a water-protein matrix of serum albumin molecules]. 836 60

We postulated that nitroimidazoles, previously used for radiosensitizing solid tumors, may be interesting templates as carriers of 10B for boron neutron capture therapy. To test this hypothesis, we synthesized a 10B-enriched nitroimidazole, 1-2[(undecahydro-closo-dodecaborato)thio]ethyl]-2- methyl-5-nitroimidazole (imidocaptate), by coupling the Cs salt of BSH (Cs2-10B12H11SH) with 1-(2-bromoethyl)-2-methyl-5-nitroimidazole followed by purification of the adduct. Imidocaptate was taken up by V-79 cells in culture and showed no inherent toxicity under euoxic conditions up to 1.05 mM (126 micrograms of 10B/mL of culture medium). Imidocaptate showed a dose-dependent decrease in D0 when the treated cells were irradiated with a thermal neutron beam. At the highest dose tested (126 micrograms of 10B/mL of culture medium), the ratio of control to sample D0 values was 2.6 for both linear quadratic and single-hit multitarget models. At 33 micrograms of 10B/mL, imidocaptate showed a control/treated D0 ration (1.5) equal to that observed with the disulfide form of BSH at 28 micrograms of 10B/mL. Compared to BSH and its disulfide, the reduced toxicity and equipotency of imidocaptate suggest that this agent may be useful for boron neutron capture therapy of cancer.
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PMID:Synthesis and evaluation of a boronated nitroimidazole for boron neutron capture therapy. 869 85

Heat-stable antigen (HSA/mouse CD24) is expressed in both haematopoietic and neural cells. The small core protein of the molecule is extensively glycosylated and anchored to the membrane via glycosylphosphatidylinositol. The role of HSA in the developing brain as well as its functional properties are poorly understood. Here we show that the brain HSA is associated with N- and O-linked oligosaccharide moieties and decorated with the HNK-1 sulfated carbohydrate epitope. It can bind P-selectin but not E-selectin and this interaction requires divalent cations and is sensitive to high salt. Brain derived HSA is also capable of binding to the L1 adhesion molecule. This interaction is distinct from the P-selectin binding as it is resistant to high salt and does not require bivalent cations. Treatment of HSA with OSGE significantly reduced binding of both P-selectin and I.1. Our data suggest that HSA can bind P-selectin and I.1 by distinct mechanism and that the binding epitopes on HSA are in close proximity.
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PMID:Heat-stable antigen (mouse CD24) in the brain: dual but distinct interaction with P-selectin and L1. 904 6

The equations for the quadrupolar relaxation of spin 3 were derived for the Redfield limit where the molecular reorientation rate is much faster than the size of the quadrupolar interaction. In the extreme narrowing regime (omega0tauc << 1), the results converge to the analytical expressions for the relaxation rates available in the literature. For slower motions, both longitudinal (spin-lattice) and transverse (spin-spin) relaxations are described by a superposition of three exponentials, where both the rates themselves and their relative weights are functions of omega0tauc. Numerical calculations of the relevant relaxation parameters in the intermediate omega0tauc regime are presented. Spin-lattice relaxation is described to very good approximation by a single exponential for all values of omega0tauc, with the weight of the dominant decay mode exceeding 0. 97 for the entire range. The predictions of these simulations were found to be in good agreement with experimentally measured relaxation rates of the 10B resonances in the sodium salt of Na2B12H12S, mercaptoundecahydro-closo-dodecaborane (sodium borocaptate or BSH) dissolved in glycerol, determined at omega0 = 53. 73 MHz, between temperatures of 268 and 323 K. The fit to the experimental results yielded a value of 1.25 MHz for the average 10B quadrupolar coupling constant in this molecule. Copyright 1997 Academic Press. Copyright 1997Academic Press
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PMID:Quadrupolar relaxation of spin 3 in the intermediate omega0tauc regime 940 11

Human biliary mucin and calcium binding protein (CBP) influence formation of both calcium salt precipitates and cholesterol crystals and colocalize in the center of cholesterol gallstones. We investigated how physiological concentrations of these proteins regulate cholesterol crystallization in model biles, supersaturated with cholesterol and calcium salts, mimicking pathological human bile. Using polarizing light microscopy and nephelometry to assess cholesterol crystallization, the influence of calcium ions and calcium phosphate precipitates in the absence and presence of mucin, CBP, and human serum albumin was determined. Calcium phosphate precipitates stimulated cholesterol crystallization more strongly than soluble calcium. Mucin also stimulated, and with soluble calcium or calcium phosphate precipitates additively increased, the cholesterol crystal mass. In the absence of mucin, only human serum albumin plus CBP, not these proteins individually, decreased the stimulating effect of calcium phosphate precipitates but not of soluble calcium. However, seeding of calcium phosphate precipitates in biles with mucins resulted in near complete cholesterol crystallization within one day whether CBP and HSA were or were not also present. In conclusion, calcium salt precipitates plus human biliary mucins induce rapid and complete crystallization of cholesterol from model biles, little influenced by human biliary calcium binding proteins.
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PMID:Mucins and calcium phosphate precipitates additively stimulate cholesterol crystallization. 974 86


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