Search results for " Albumin"
showing 10 items of 320 documents
Flavour retention and release from protein solutions
2006
International audience; This paper briefly presents the main results obtained up to now on protein–flavour binding and release in relation with flavour perception. Among the food proteins, β-lactoglobulin is the most extensively studied for its binding properties, which involve both hydrophobic and hydrogen binding. Recent developments using molecular modelling and Quantitative Structure–Activity Relationship confirmed the existence of two different binding sites for flavour compounds on β-lactoglobulin. During the aroma release process in the mouth, not only free aroma compounds are released but also those reversibly bound by the protein, pointing out the fact that flavour perception is on…
Widespread diminishing anthropogenic effects on calcium in freshwaters
2019
Calcium (Ca) is an essential element for almost all living organisms. Here, we examined global variation and controls of freshwater Ca concentrations, using 440 599 water samples from 43 184 inland water sites in 57 countries. We found that the global median Ca concentration was 4.0 mg L−1 with 20.7% of the water samples showing Ca concentrations ≤ 1.5 mg L−1 , a threshold considered critical for the survival of many Ca-demanding organisms. Spatially, freshwater Ca concentrations were strongly and proportionally linked to carbonate alkalinity, with the highest Ca and carbonate alkalinity in waters with a pH around 8.0 and decreasing in concentrations towards lower pH. However, on a temporal…
Serum Albumin and Future Risk of Hip, Humeral, and Wrist Fractures in Caucasian Men : New Findings from a Prospective Cohort Study
2019
Objective: Low serum albumin concentration is associated with poor health outcomes, but its relationship with the risk of fractures has not been reliably quantified. We aimed to assess the prospective association of serum albumin with the risk of fractures in a general population. Subjects and Methods: Baseline serum albumin concentrations were measured in 2,245 men aged 42–61 years in the Kuopio Ischemic Heart Disease study. Hazard ratios (HRs) (95% confidence intervals) were calculated for incident fractures. Results: A total of 121 fractures (hip, humeral, or wrist) were recorded during a median follow-up of 25.6 years. The risk of fractures increased linearly below a serum albumin conc…
Potential anticarcinogenic peptides from bovine milk.
2012
Bovine milk possesses a protein system constituted by two major families of proteins: caseins (insoluble) and whey proteins (soluble). Caseins (αS1,αS2,β, andκ) are the predominant phosphoproteins in the milk of ruminants, accounting for about 80% of total protein, while the whey proteins, representing approximately 20% of milk protein fraction, includeβ-lactoglobulin,α-lactalbumin, immunoglobulins, bovine serum albumin, bovine lactoferrin, and lactoperoxidase, together with other minor components. Different bioactivities have been associated with these proteins. In many cases, caseins and whey proteins act as precursors of bioactive peptides that are released, in the body, by enzymatic pro…
The deubiquitinase USP11 is a versatile and conserved regulator of autophagy
2021
Autophagy is a major cellular quality control system responsible for the degradation of proteins and organelles in response to stress and damage to maintain homeostasis. Ubiquitination of autophagy-related proteins or regulatory components is important for the precise control of autophagy pathways. Here, we show that the deubiquitinase ubiquitin-specific protease 11 (USP11) restricts autophagy and that KO of USP11 in mammalian cells results in elevated autophagic flux. We also demonstrate that depletion of the USP11 homolog H34C03.2 in Caenorhabditis elegans triggers hyperactivation of autophagy and protects the animals against human amyloid-β peptide 42 aggregation-induced paralysis. USP11…
Thermal aggregation of proteins in presence of metal ions.
2008
The study of the aggregation processes in presence of metal ions is an essential step for understanding the key role of metals in protein-protein and protein-solvent interactions. Indeed, the presence of metal ions can radically change the main features of the standard denaturation/aggregation processes and such effects result to be strongly dependent on the kind of metal and on its concentration. Metal ions have an active role in thermal aggregation and cold set gelation processes. These processes are intrinsically different, but both are based on the proteins ability to form aggregates.
Spectroscopic studies of water-soluble superstructured iron(III) porphyrin. Interaction with the bovine serum albumin protein
2018
Acid-base equilibrium of the “one-face”-hindered sulfonated porphyrin, α5,15-[2,2′(dodecamethyleneoxy),(5-sulfonato)diphenyl]-10,20-bis(2-hydroxy,5-sulfonatophenyl)porphyrinato iron(III), has been ...
Drug Binding Properties of Tyrosine-Modified Human Serum Albumin
1978
Human serum albumin (HSA) has only a small number of specific binding sites for drugs. There are facts indicating that tyrosine residues may be involved in these binding sites. Thus we modified HSA with tetranitromethan, a reagent specific for tyrosine residues in proteins. As derived from an UV-absorption quotient three albumins with a degree of modification of two, five and eight residues per molecule were obtained. Only for the albumin with eight residues modified a small reduction of ordered secondary structure was found.
Protein transport through gold-coated, charged nanopores: Effects of applied voltage
2006
The flux of bovine serum albumin and bovine hemoglobin through charged nanopores inside polymeric membranes is analysed as a function of the applied voltage to the nanopore surface, the solution ionic strength and pH. The electrostatic interaction of the protein with the nanopore surface gives low transport rates except at the protein isoelectric point and the minimum of the effective, voltage-induced nanopore charge. This electrostatic sieving effect allows for the separation of proteins with similar molecular weights.
Surface Modification of Porous Polyethylene Implants with an Albumin-Based Nanocarrier-Release System
2021
Background: Porous polyethylene (PPE) implants are used for the reconstruction of tissue defects but have a risk of rejection in case of insufficient ingrowth into the host tissue. Various growth factors can promote implant ingrowth, yet a long-term gradient is a prerequisite for the mediation of these effects. As modification of the implant surface with nanocarriers may facilitate a long-term gradient by sustained factor release, implants modified with crosslinked albumin nanocarriers were evaluated in vivo. Methods: Nanocarriers from murine serum albumin (MSA) were prepared by an inverse miniemulsion technique encapsulating either a low- or high-molar mass fluorescent cargo. PPE implants …