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- Isaksson, M., et al.
(författare)
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Determination of the retention of 47Ca by whole-body counting
- 2000
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Ingår i: Applied Radiation and Isotopes. - 0969-8043 .- 1872-9800. ; 52:6, s. 1441-1450
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Tidskriftsartikel (refereegranskat)abstract
- Retention of intravenously or orally administered 47Ca in the human body are described by a two-parameter function. It is then sufficient to make only a few whole-body measurements to determine the retention function, avoiding faeces sampling and stool markers. Seven days after intake the non-absorbed calcium was excreted and the model agreed with the measured relative retention. Absorption of calcium could then, in some cases (e.g. comparative studies), be described by relative retention at the 7th day after intake. Copyright (C) 2000 Elsevier Science Ltd.
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| 2. |
- Isaksson, Sven, et al.
(författare)
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Temperature-dependent dielectric properties of foods during freezing and thawing
- 2017
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Ingår i: 16th International Conference on Microwave and High Frequency Heating, AMPERE 2017.
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Konferensbidrag (refereegranskat)abstract
- Dielectric properties of a variety of foodstuffs were measured during freezing and thawing conditions, and are presented here as functions of temperature. Measurements were done with the Agilent 85070 high temperature dielectric probe. The differences in characteristics of the graphs resulting from cooling and thawing are discussed. A specific model accommodating the amount of frozen water in the food sample as a function of temperature is used and compared to experimental results. The mass fraction of each component is coupled to the dielectric properties of each fraction to evaluate the effective dielectric properties based on a two phases Maxwell-Wagner model considering ice as a dispersed fraction and food as a continuous fraction. The unknown dielectric properties of dry matter and an adjusting coefficient are used to optimize the fitting between experimental data and calculated data.
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| 3. |
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| 4. |
- Le-Bail, A., et al.
(författare)
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Freezewave; A new European project on freezing under microwaves irradiation
- 2018
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Ingår i: Refrigeration Science and Technology. - 9782362150241 ; , s. 182-189
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Konferensbidrag (refereegranskat)abstract
- FREEZEWAVE project is an ERANET SUSFOOD project (May 2015 - Dec. 2018). It concerns the freezing of foods using a highly innovative technique combining freezing at slow rate with part time emission of microwaves (2450 MHz); this innovative concept has been investigated recently by ONIRIS and results showed that a 62% decrease of the average ice crystal size was acquired when samples were frozen under microwave irradiation compared to the control (Xanthakis et al., 2014, IFSET - study on pork meat). To improve the quality of frozen foods, fast freezing is usually recommended, resulting in a reduction of the ice crystals. However, a fast freezing increases the energy demand: low ambient temperature & high air velocity to enhance the rate of heat transfer are needed to achieve a fast freezing. FREEZEWAVE project aims at expanding & optimizing the concept to several foods (sauce, meat, vegetable & ready to eat meals) and also at designing industrial equipment. The novel concept concerns the freezing equipment sector thanks to a French SME partner (SAIREM) and the global frozen food sector. FREEZEWAVE will provide scientific knowledge and new scientific insights in food freezing. Project's outcomes may also be of interest for non-food applications such as biotechnology.
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| 5. |
- Sivertsen, A, et al.
(författare)
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Synthetic cationic antimicrobial peptides bind with their hydrophobic parts to drug site II of human serum albumin
- 2014
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Ingår i: BMC Structural Biology. - : Springer Science and Business Media LLC. - 1472-6807. ; 14:1
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Tidskriftsartikel (refereegranskat)abstract
- Background Many biologically active compounds bind to plasma transport proteins, and this binding can be either advantageous or disadvantageous from a drug design perspective. Human serum albumin (HSA) is one of the most important transport proteins in the cardiovascular system due to its great binding capacity and high physiological concentration. HSA has a preference for accommodating neutral lipophilic and acidic drug-like ligands, but is also surprisingly able to bind positively charged peptides. Understanding of how short cationic antimicrobial peptides interact with human serum albumin is of importance for developing such compounds into the clinics. Results The binding of a selection of short synthetic cationic antimicrobial peptides (CAPs) to human albumin with binding affinities in the μM range is described. Competitive isothermal titration calorimetry (ITC) and NMR WaterLOGSY experiments mapped the binding site of the CAPs to the well-known drug site II within subdomain IIIA of HSA. Thermodynamic and structural analysis revealed that the binding is exclusively driven by interactions with the hydrophobic moieties of the peptides, and is independent of the cationic residues that are vital for antimicrobial activity. Both of the hydrophobic moieties comprising the peptides were detected to interact with drug site II by NMR saturation transfer difference (STD) group epitope mapping (GEM) and INPHARMA experiments. Molecular models of the complexes between the peptides and albumin were constructed using docking experiments, and support the binding hypothesis and confirm the overall binding affinities of the CAPs. Conclusions The biophysical and structural characterizations of albumin-peptide complexes reported here provide detailed insight into how albumin can bind short cationic peptides. The hydrophobic elements of the peptides studied here are responsible for the main interaction with HSA. We suggest that albumin binding should be taken into careful consideration in antimicrobial peptide studies, as the systemic distribution can be significantly affected by HSA interactions.
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