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The Israel Medical Association Journal... Jan 2006
Review
Topics: Adult; Aged; Blood Proteins; Case-Control Studies; Factor V; Humans; Middle Aged; Stroke; Thrombosis
PubMed: 16450754
DOI: No ID Found -
PloS One 2018Phospholipases A2 (PLA2) are enzymes acting on the cell membrane phospholipids resulting in fatty acids and lysophospholipids and deconstructing the cell membrane. This...
Phospholipases A2 (PLA2) are enzymes acting on the cell membrane phospholipids resulting in fatty acids and lysophospholipids and deconstructing the cell membrane. This protein is commonly found in snake venoms, causing tissue inflammation in the affected area. Evidence indicates that snakes have natural resistance to their own venom due to protective properties in plasma, that inhibit the action of proteins present in their venom. Given that, this study aimed to purify and characterize a γPLI from Bothrops jararaca serum, named γBjPLI. PLA2 inhibitor was isolated using two chromatographic steps: an ion exchange column (DEAE), followed by an affinity column (crotoxin coupled to a CNBr-activated Sepharose resin). The purity and biochemical characterization of the isolated protein were analyzed by RP-HPLC, SEC, SDS-PAGE, circular dichroism and mass spectrometry. The ability to inhibit PLA2 was determined by enzymatic activity, neutralization of paw edema and myonecrosis. The protein purity was confirmed by RP-HPLC and SEC, whilst an apparent molecular mass of 25 kDa and 20 kDa was obtained by SDS-PAGE, under reducing and non-reducing conditions, respectively. According to mass spectrometry analysis, this protein showed 72% and 68% of coverage when aligned to amino acid sequences of two proteins already described as PLIs. Thus, the inhibitory activity of enzymatic, edema and myonecrotic activities by γBjPLI suggests a role of this inhibitor for protection of these snakes against self-envenomation.
Topics: Animals; Blood Proteins; Bothrops; Phospholipase A2 Inhibitors; Phospholipases A2; Reptilian Proteins
PubMed: 29505564
DOI: 10.1371/journal.pone.0193105 -
Bacteriological Reviews Jun 1977
Review
Topics: Animals; Antibodies, Bacterial; Bacillus subtilis; Bacteria; Blood Bactericidal Activity; Blood Platelets; Blood Proteins; Cell Membrane; Cell Wall; Hot Temperature; Humans; Muramidase; Protein Denaturation; Species Specificity
PubMed: 407899
DOI: 10.1128/br.41.2.501-513.1977 -
Journal of Clinical Pathology.... 1970
Review
Topics: Alpha-Globulins; Animals; Basal Metabolism; Blood Proteins; Burns; Carbon Isotopes; Dogs; Environmental Exposure; Fibrin; Fibrinogen; Fractures, Bone; Humans; Iodine Isotopes; Nitrogen; Nitrogen Isotopes; Paralysis; Postoperative Complications; Proteins; Rats; Serum Albumin; Serum Albumin, Radio-Iodinated; Temperature; Wounds and Injuries; gamma-Globulins
PubMed: 4123923
DOI: 10.1136/jcp.s3-4.1.56 -
Antioxidants & Redox Signaling Feb 2010Hemoglobin biosynthesis in erythrocyte precursors involves several steps. The correct ratios and concentrations of normal alpha (alpha) and beta (beta) globin proteins... (Review)
Review
Hemoglobin biosynthesis in erythrocyte precursors involves several steps. The correct ratios and concentrations of normal alpha (alpha) and beta (beta) globin proteins must be expressed; apoproteins must be folded correctly; heme must be synthesized and incorporated into these globins rapidly; and the individual alpha and beta subunits must be rapidly and correctly assembled into heterotetramers. These events occur on a large scale in vivo, and dysregulation causes serious clinical disorders such as thalassemia syndromes. Recent work has implicated a conserved erythroid protein known as Alpha-Hemoglobin Stabilizing Protein (AHSP) as a participant in these events. Current evidence suggests that AHSP enhances alpha subunit stability and diminishes its participation in harmful redox chemistry. There is also evidence that AHSP facilitates one or more early-stage post-translational hemoglobin biosynthetic events. In this review, recent experimental results are discussed in light of several current models describing globin subunit folding, heme uptake, assembly, and denaturation during hemoglobin synthesis. Particular attention is devoted to molecular interactions with AHSP that relate to alpha chain oxidation and the ability of alpha chains to associate with partner beta chains.
Topics: Animals; Blood Proteins; Hemoglobins; Humans; Models, Biological; Molecular Chaperones; Oxidation-Reduction; Protein Binding; Protein Structure, Secondary
PubMed: 19659437
DOI: 10.1089/ars.2009.2780 -
Analytical Chemistry Jan 2016Among human body fluids, serum plays a key role for diagnostic tests and, increasingly, for metabolomics analysis. However, the high protein content of serum poses...
Among human body fluids, serum plays a key role for diagnostic tests and, increasingly, for metabolomics analysis. However, the high protein content of serum poses significant challenges for nuclear magnetic resonance (NMR)-based metabolomics studies because it can strongly interfere with metabolite signal detection and quantitation. Although several methods for protein removal have been proposed, including ultrafiltration and organic-solvent-induced protein precipitation, there is currently no standard operating procedure for the elimination of protein from human serum samples. Here, we introduce novel procedures for the removal of protein from serum by the addition of nanoparticles. It is demonstrated how serum protein can be efficiently, cost-effectively, and environmentally friendly removed at physiological pH (pH 7.4) through attractive interactions with silica nanoparticles. It is further shown how serum can be processed with nanoparticles prior to ultrafiltration or organic-solvent-induced protein precipitation for optimal protein removal. After examination of all of the procedures, the combination of nanoparticle treatment and ultrafiltration is found to have a minimal effect on the metabolite content, leading to remarkably clean homo- and heteronuclear NMR spectra of the serum metabolome that compare favorably to other methods for protein removal.
Topics: Blood Proteins; Humans; Metabolomics; Nanoparticles; Nuclear Magnetic Resonance, Biomolecular
PubMed: 26605638
DOI: 10.1021/acs.analchem.5b03889 -
BioTechniques Jan 2024This study computationally evaluates the molecular docking affinity of various perfluoroalkyl and polyfluoroalkyl substances (PFAs) towards blood proteins using a...
This study computationally evaluates the molecular docking affinity of various perfluoroalkyl and polyfluoroalkyl substances (PFAs) towards blood proteins using a generative machine-learning algorithm, DiffDock, specialized in protein-ligand blind-docking learning and prediction. Concerns about the chemical pathways and accumulation of PFAs in the environment and eventually in the human body has been rising due to empirical findings that levels of PFAs in human blood has been rising. DiffDock may offer a fast approach in determining the fate and potential molecular pathways of PFAs in human body.
Topics: Humans; Artificial Intelligence; Molecular Docking Simulation; Algorithms; Blood Proteins; Fluorocarbons
PubMed: 37947020
DOI: 10.2144/btn-2023-0070 -
The Journal of Clinical Investigation Nov 1990
Review
Topics: Amino Acid Sequence; Animals; Antimicrobial Cationic Peptides; Bacteria; Bacterial Physiological Phenomena; Blood Proteins; Carrier Proteins; Cathepsin G; Cathepsins; Defensins; Humans; Molecular Sequence Data; Neutrophils; Phagocytosis; Serine Endopeptidases
PubMed: 2243118
DOI: 10.1172/JCI114851 -
Angewandte Chemie (International Ed. in... Mar 2020Amphiphilic surface groups play an important role in many biological processes. The synthesis of amphiphilic polyphenylene dendrimer branches (dendrons), providing...
Amphiphilic surface groups play an important role in many biological processes. The synthesis of amphiphilic polyphenylene dendrimer branches (dendrons), providing alternating hydrophilic and lipophilic surface groups and one reactive ethynyl group at the core is reported. The amphiphilic surface groups serve as biorecognition units that bind to the surface of adenovirus 5 (Ad5), which is a common vector in gene therapy. The Ad5/dendron complexes showed high gene transduction efficiencies in coxsackie-adenovirus receptor (CAR)-negative cells. Moreover, the dendrons offer incorporation of new functions at the dendron core by in situ post-modifications, even when bound to the Ad5 surface. Surfaces coated with these dendrons were analyzed for their blood-protein binding capacity, which is essential to predict their performance in the blood stream. A new platform for introducing bioactive groups to the Ad5 surface without chemically modifying the virus particles is provided.
Topics: Adenoviridae; Animals; Blood Proteins; CHO Cells; Cell Survival; Cricetinae; Cricetulus; Cycloaddition Reaction; Dendrimers; Hydrophobic and Hydrophilic Interactions; Liposomes; Polymers; Protein Binding; Surface Properties
PubMed: 31943635
DOI: 10.1002/anie.201913708 -
British Journal of Pharmacology Sep 19711. By combining the agar plate diffusion technique for determination of antibiotic activity and zone microelectrophoresis in agar gel, the activity of fusidic acid in...
1. By combining the agar plate diffusion technique for determination of antibiotic activity and zone microelectrophoresis in agar gel, the activity of fusidic acid in individual serum proteins of blood and pus obtained from patients given sodium fusidate revealed albumin to be responsible for the protein binding of this antibiotic.2. Based on the assumption that only free fusidic acid is microbiologically active, the relationship between the concentration of albumin and the ratio of free to total fusidic acid was determined at four concentrations of free fusidic acid, using as test organisms four differently sensitive variants of a Staphylococcus aureus strain. At each concentration an increasing amount of albumin (0-40 mg/ml culture medium) decreased the activity of fusidic acid as determined in serial dilutions (IC50).3. The law of mass action expressed as Langmuir's adsorption isotherm was valid if a correction for the influence of albumin on the sensitivity of the strain of Staph. aureus was introduced. For other test organisms no correction is necessary. The constant in Langmuir's adsorption isotherm was K=78400+/-8200 l./mol and n=3.15 (95% confidence limits: 2.09-5.52).4. The mean blood concentration was 20.8 mug/ml and the mean pus concentration 17.2 mug/ml in nineteen sets of blood and pus samples. The ratio of pus to blood corresponds to the ratio of published values for the protein concentrations in serum and in inflammatory oedema.5. It is concluded that for albumin bound drugs the ;storage depot' of the organism also includes the fluid of the tissue spaces including the inflammatory oedema. As recent studies have revealed an extravascular albumin pool similar in size to the plasma pool, this ;storage depot' should not be neglected.
Topics: Agar; Blood Protein Electrophoresis; Blood Proteins; Drug Interactions; Fusidic Acid; Gels; Humans; Kinetics; Models, Chemical; Protein Binding; Serum Albumin; Staphylococcus; Suppuration
PubMed: 5136455
DOI: 10.1111/j.1476-5381.1971.tb07164.x