scholarly journals Immune reactions in polysaccharide media. Investigation on complex-formation between some polysaccharides, albumin and immunoglobulin G

1969 ◽  
Vol 112 (4) ◽  
pp. 483-487 ◽  
Author(s):  
Krister Hellsing
Keyword(s):  
Sodium Chloride ◽  
Complex Formation ◽  
Serum Albumin ◽  
Immunoglobulin G ◽  
Phosphate Buffer ◽  
Equilibrium Dialysis ◽  
Immune Reactions ◽  
Precipitin Reaction ◽  
Specific Complex

Serum albumin and immunoglobulin G were chromatographed on columns of dextran, hyaluronate and chondroitin 4-sulphate. The partition of the two proteins between hyaluronate and buffer was also measured by equilibrium dialysis. The results accord with the view that there is no complex-formation between the polysaccharides and the proteins in 0·05m-phosphate buffer, pH7·4, containing sodium chloride (0·1m). The observations support the hypothesis that the previously described polysaccharide enhancement of the precipitin reaction is due to exclusion and not to non-specific complex-formation.

scholarly journals Immune reactions in polysaccharide media. Polysaccharide-enhanced precipitin reactions with antigens of various sizes

1969 ◽  
Vol 114 (1) ◽  
pp. 145-149 ◽  
Author(s):  
Krister Hellsing
Keyword(s):  
Serum Albumin ◽  
Immunoglobulin G ◽  
Immune Complexes ◽  
Immune Reactions ◽  
Precipitin Reaction ◽  
Steric Exclusion ◽  
Molecular Sizes

The influence of the size of the antigen in the polysaccharide-enhanced precipitin reaction was investigated. The experiments were carried out by addition of homologous antigens of different molecular sizes (the monomer, dimer and trimer of serum albumin and the monomer and dimer of immunoglobulin G) to the same preparation of antibody in the absence and presence of dextran. Dextran decreased the solubility of the immune complexes to a larger extent when the antigen size increased. This is in accord with the view that the polysaccharide effect is due to steric exclusion.

scholarly journals Immune reactions in polysaccharide media. The composition of the antigen–antibody complexes in the precipitin reaction

1969 ◽  
Vol 114 (1) ◽  
pp. 141-144 ◽  
Author(s):  
Krister Hellsing
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Immunoglobulin G ◽  
Immune Complexes ◽  
Aggregate Size ◽  
Precipitin Reaction ◽  
Soluble Immune Complexes ◽  
Immune Aggregates ◽  
Antigen Antibody ◽  
Free Antigen

The precipitin reaction is enhanced in the presence of polysaccharides (Hellsing, 1966). This reaction has now been studied in detail with labelled antigen (125I-labelled human serum albumin) and antibody (131I-labelled rabbit anti-albumin immunoglobulin G). The relative proportions of antigen and antibody in the precipitates are unchanged by the addition of dextran in spite of the increased precipitation. The ratio of antibody to antigen in the soluble immune complexes decreases with increasing polysaccharide concentration. This can be interpreted as a decrease in the aggregate size of the complexes. At the same time the amount of free antigen in the solution increases. The results are consistent with a decrease in solubility, primarily of the large immune aggregates, together with a shift in the equilibrium between small and large complexes. The effect is in accord with a steric-exclusion phenomenon.

scholarly journals Formation of Nanocomplexes between Carboxymethyl Inulin and Bovine Serum Albumin via pH-Induced Electrostatic Interaction

Molecules ◽  
2019 ◽  
Vol 24 (17) ◽  
pp. 3056 ◽  
Author(s):  
Guiying Huang ◽  
Jun Liu ◽  
Weiping Jin ◽  
Zihao Wei ◽  
Chi-Tang Ho ◽  
...  
Keyword(s):  
Sodium Chloride ◽  
Bovine Serum Albumin ◽  
Complex Formation ◽  
Serum Albumin ◽  
Electrostatic Interaction ◽  
Bovine Serum ◽  
Titration Calorimetry ◽  
Food Ingredients ◽  
Enthalpy Changes ◽  
Ft Ir

As a functional polysaccharide, inulin was carboxymethylated and it formed nanocomplexes with bovine serum albumin (BSA). The success of obtaining carboxymethyl inulin (CMI) was confirmed by a combination of Fourier transform Infrared (FT-IR), Raman spectroscopy, gel permeation chromatography (GPC), and titration. The effects of pH and ionic strength on the formation of CMI/BSA nanocomplexes were investigated. Our results showed that the formation of complex coacervate (pHφ1) and dissolution of CMI/BSA insoluble complexes (pHφ2) appeared in pH near 4.85 and 2.00 respectively. FT-IR and Raman data confirmed the existence of electrostatic interaction and hydrogen bonding between CMI and BSA. The isothermal titration calorimetry (ITC) results suggested that the process of complex formation was spontaneous and exothermic. The complexation was dominated by enthalpy changes (∆Η < 0, ∆S < 0) at pH 4.00, while it was contributed by enthalpic and entropic changes (∆Η < 0, ∆S > 0) at pH 2.60. Irregularly shaped insoluble complexes and globular soluble nanocomplexes (about 150 nm) were observed in CMI/BSA complexes at pH 4.00 and 2.60 while using optical microscopy and atomic force microscopy, respectively. The sodium chloride suppression effect on CMI/BSA complexes was confirmed by the decrease of incipient pH for soluble complex formation (or pHc) and pHφ1 under different sodium chloride concentrations. This research presents a new functional system with the potential for delivering bioactive food ingredients.

scholarly journals Immune reactions in polysaccharide media. Experiments with specific antibodies of different affinities for serum albumin

1969 ◽  
Vol 114 (1) ◽  
pp. 151-155 ◽  
Author(s):  
Krister Hellsing
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Rabbit Antibody ◽  
Immune Reactions ◽  
Specific Antibodies ◽  
Precipitin Reaction ◽  
Immune Precipitation ◽  
Exclusion Mechanism ◽  
Immunological Assays

Rabbit antibody fractions of different affinities for human serum albumin were prepared by an immunosorbent technique. The fractions were used in studies on the enhancement of the precipitin reaction by polymers. Dextran increased the immune precipitation to about the same extent regardless of whether antibodies with high and low affinities were used. The effect should considerably facilitate the detection of antibodies with low precipitating ability in immunological assays. The results are discussed in terms of a steric-exclusion mechanism.

Bioceramic Hydroxyapatite Granules for Purification of Biotechnological Products

2011 ◽  
Vol 284-286 ◽  
pp. 1764-1769 ◽  
Author(s):  
Vitalijs Lakevics ◽  
Janis Locs ◽  
Dagnija Loca ◽  
Valentina Stepanova ◽  
Liga Berzina-Cimdina ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Phosphate Buffer ◽  
Bovine Serum ◽  
Phosphate Buffer Solution ◽  
Sorption Process ◽  
Buffer Solution ◽  
Ph Values ◽  
Bovine Serum Albumin Adsorption ◽  
Albumin Adsorption

Sorption experiments of bovine serum albumin (BSA) on hydroxyapatite (HAp) ceramic granules, prepared at three temperatures 900°C, 1000°C and 1150°C were performed at room temperature 18,6 °C and phosphate buffer, pH 5,83; 6.38 and 7,39. Thermal treatment contributed to the decrease of bovine serum albumin immobilization indicating that sorption process depended on HAp ceramics specific surface area and pH values of phosphate buffer solution. However, it was confirmed that granule size was also an important parameter for bovine serum albumin adsorption. As a result of these experiments, the most appropriate adsorption conditions and phosphate buffer pH values influence on to BSA sorption were analyzed.

scholarly journals Electrochemical characterization and determination of carbamazepine as pharmaceutical standard and tablet content on gold electrode

2014 ◽  
Vol 68 (2) ◽  
pp. 207-212 ◽  
Author(s):  
Nemanja Trisovic ◽  
Bojan Bozic ◽  
Slobodan Petrovic ◽  
Svetlana Tadic ◽  
Milka Avramov-Ivic
Keyword(s):  
Cyclic Voltammetry ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Phosphate Buffer ◽  
Bovine Serum ◽  
Gold Electrode ◽  
Anticonvulsant Drug ◽  
Voltammetric Techniques ◽  
Anodic Behaviour

The anodic behaviour of carbamazepine (CBZ), an anticonvulsant drug, has been studied on gold electrode in 0.1 mol dm-3 phosphate buffer of pH 7.0 by using cyclic voltammetry. It has been found that the value of the oxidative current of pure CBZ at +0.90 V is a linear function of the concentration in a range from 1.0?10-7 to 1.0?10?4 mol dm?3. The detection of CBZ in the concentration of 1.0?10-8 mol dm-3 is among the lowest that have been reported for this drug using voltammetric techniques. CBZ as a content of tablet Galepsine? has been quantitatively determined. It has also been demonstrated that the modification of gold electrode with bovine serum albumin (BSA) results in a decrease of the oxidative peak current due to the binding of the drug to BSA.

COMPLEX FORMATION BETWEEN BASIC ANTIBIOTICS AND DEOXYRIBONUCLEIC ACID IN HUMAN PULMONARY SECRETIONS

PEDIATRICS ◽  
1965 ◽  
Vol 36 (5) ◽  
pp. 714-720
Author(s):  
Joseph L. Potter ◽  
LeRoy W. Matthews ◽  
Samuel Spector ◽  
Joy Lemm
Keyword(s):  
Cystic Fibrosis ◽  
Sodium Chloride ◽  
Complex Formation ◽  
Chain Length ◽  
Deoxyribonucleic Acid ◽  
Antimicrobial Agents ◽  
Dnase I ◽  
Two Samples

1. Complex formation and precipitation of DNA by neomycin, with consequent inactivation of the antibiotic, has been shown to occur in the pulmonary secretions of patients with cystic fibrosis. 2. Highly polymerized DNA from a variety of sources, as well as two samples of RNA, were precipitated by neomycin in vitro. Polymixin, kanamycin, colymycin, and streptomycin similarly co-precipitate with DNA in vitro. 3. The minimum chain length of polynucleotide required for precipitation in the DNA-neomycin system was 10. 4. The complex is readily attacked by DNase I resulting in the splitting of the DNA and the liberation of the antibiotic. Both components of the complex are solubilized in M sodium chloride. 5. The resistance of purulent foci of infection to therapy with basic antimicrobial agents may, in part, be due to the complex formation with the high levels of DNA found at the site of infection.

Heteroprotein complex formation of bovine serum albumin and lysozyme: Structure and thermal stability

2018 ◽  
Vol 74 ◽  
pp. 267-274 ◽  
Author(s):  
Monique Barreto Santos ◽  
Carlos Wanderlei Piler de Carvalho ◽  
Edwin Elard Garcia-Rojas
Keyword(s):  
Thermal Stability ◽  
Bovine Serum Albumin ◽  
Complex Formation ◽  
Serum Albumin ◽  
Bovine Serum

Binding of cadmium(II) and zinc(II) to human and dog serum albumins. An equilibrium dialysis and 113Cd-NMR study

1991 ◽  
Vol 69 (12) ◽  
pp. 809-820 ◽  
Author(s):  
William Goumakos ◽  
Jean-Pierre Laussac ◽  
Bibudhendra Sarkar
Keyword(s):  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Metal Ion ◽  
Equilibrium Dialysis ◽  
Scatchard Analysis ◽  
Serum Albumins ◽  
High Affinity ◽  
Nmr Study ◽  
Nmr Techniques

The binding of Cd(II) and Zn(II) to human serum albumin (HSA) and dog serum albumin (DSA) has been studied by equilibrium dialysis and 113Cd(II)-NMR techniques at physiological pH. Scatchard analysis of the equilibrium dialysis data indicate the presence of at least two classes of binding sites for Cd(II) and Zn(II). On analysis of the high-affinity class of sites, HSA is shown to bind 2.08 ± 0.09 (log K = 5.3 ± 0.6) and 1.07 ± 0.12 (log K = 6.4 ± 0.8) moles of Cd(II) and Zn(II) per mole of protein, respectively. DSA bound 2.02 ± 0.19 (log K = 5.1 ± 0.8), and 1.06 ± 0.15 (log K = 6.0 ± 0.2) moles of Cd(II) and Zn(II) per mole of protein, respectively. Competition studies indicate the presence of one high-affinity Cd(II) site on both HSA and DSA that is not affected by Zn(II) or Cu(II), and one high-affinity Zn(II) site on both HSA and DSA that is not affected by Cd(II) or Cu(II). 113Cadmium-HSA spectra display three resonances corresponding to three different sites of complexation. In site I, Cd(II) is most probably coordinated to two or three histidyl residues, site II to one histidyl residue and three oxygen ligands (carboxylate), while for the most upfield site III, four oxygens are likely to be involved in the binding of the metal ion. The 113Cd(II)-DSA spectra display only two resonances corresponding to two different sites of complexation. The environment around Cd(II) at sites I and II on DSA is similar to sites I and II, respectively, on HSA. No additional resonances are observed in any of these experiments and in particular in the low field region where sulfur coordination occurs. Overall, our results are consistent with the proposal that the physiologically important high-affinity Zn(II) and Cd(II) binding sites of albumins are located not at the Cu(II)-specific NH2-terminal site, but at internal sites, involving mostly nitrogen and oxygen ligands and no sulphur ligand.Key words: albumin, human serum, dog serum, cadmium, zinc, copper, NMR, equilibrium dialysis, binding.

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