Effect of animal age on the nutritional and physicochemical qualities of ovine bresaola.

Bresaola made from New Zealand mutton and lamb, were compared in quality attributes. Mutton bresaola had slightly lower protein and higher moisture contents, and similar amount of intramuscular fat and instrumental colour compared to that of the lamb. 36 and 80 unique endogenous peptides were observed in mutton and lamb, respectively.

Physicochemical and sensory characterization of gnocchi and the effects of novel formulation on in vitro digestibility.

Conventional gnocchi are small Italian dumplings made from potatoes, flour, and eggs. In this study, a range of gnocchi-type products containing navy bean and beef meat (10-40% w/w) were developed. The nutritional, physicochemical and sensory properties of the formulated gnocchi were determined, and a Modified in vitro Stomach Stir Tank (MISST) system was used to determine in vitro digestibility.

Carbohydrate mouth rinsing has no effect on power output during cycling in a glycogen-reduced state.

Background: The effect of mouth rinsing with a carbohydrate (CHO) solution on exercise performance is inconclusive with no benefits observed in the fed state. This study examined the effect of CHO mouth rinse or CHO ingestion on performance in 9 moderately trained male cyclists.

Methods: Four trials were undertaken, separated by 7 days, in a randomized, counterbalanced design.

Listening to music can influence hedonic and sensory perceptions of gelati.

The dominant taste sensations of three different types of chocolate gelati (milk chocolate, dark chocolate, and bittersweet chocolate) were determined using forty five trained panellists exposed to a silent reference condition and three music samples differing in hedonic ratings. The temporal dominance of sensations (TDS) method was used to measure temporal taste perceptions. The emotional states of panellists were measured after each gelati-music pairing using a scale specifically developed for this study.

Analysis of free fractions for chiral drugs using ultrafast extraction and multi-dimensional high-performance affinity chromatography.

A multi-dimensional chromatographic approach was developed to measure the free fractions of drug enantiomers in samples that also contained a binding protein or serum. This method, which combined ultrafast affinity extraction with a chiral stationary phase, was demonstrated using the drug warfarin and the protein human serum albumin.

CHROMATOGRAPHIC ANALYSIS OF DRUG INTERACTIONS IN THE SERUM PROTEOME.

The binding of drugs with serum proteins and binding agents such as human serum albumin, α-acid glycoprotein, and lipoproteins is an important process in determining the activity and fate of many pharmaceuticals in the body. A variety of techniques have been used to study drug interactions with serum proteins, but there is still a need for faster or better methods for such work. High-performance liquid chromatography (HPLC) is one tool that has been utilized in many formats for these types of measurements.

High-throughput analysis of drug dissociation from serum proteins using affinity silica monoliths.

A noncompetitive peak decay method was used with 1 mm×4.6 mm id silica monoliths to measure the dissociation rate constants (kd) for various drugs with human serum albumin (HSA) and α1-acid glycoprotein (AGP). Flow rates up to 9 mL/min were used in these experiments, resulting in analysis times of only 20-30 s.

The role of oral processing in dynamic sensory perception.

Food oral processing is not only important for the ingestion and digestion of food, but also plays an important role in the perception of texture and flavor. This overall sensory perception is dynamic and occurs during all stages of oral processing. However, the relationships between oral operations and sensory perception are not yet fully understood.

Characterization of drug interactions with serum proteins by using high-performance affinity chromatography.

The binding of drugs with serum proteins can affect the activity, distribution, rate of excretion, and toxicity of pharmaceutical agents in the body. One tool that can be used to quickly analyze and characterize these interactions is high-performance affinity chromatography (HPAC). This review shows how HPAC can be used to study drug-protein binding and describes the various applications of this approach when examining drug interactions with serum proteins.

Use of peak decay analysis and affinity microcolumns containing silica monoliths for rapid determination of drug-protein dissociation rates.

This report examined the use of silica monoliths in affinity microcolumns containing human serum albumin (HSA) to measure the dissociation rates for various drugs from this protein. Immobilized HSA and control monolith columns with dimensions of 1 mm × 4.6 mm i.

Evaluation of affinity microcolumns containing human serum albumin for rapid analysis of drug-protein binding.

This study examined the use of affinity microcolumns as tools for the rapid analysis and high-throughput screening of drug-protein binding. The protein used was immobilized human serum albumin (HSA) and the model analytes were warfarin and L-tryptophan, two solutes often used as site-specific probes for drug binding to Sudlow sites I and II of HSA, respectively. The use of HSA microcolumns in binding studies was examined by using both zonal elution and frontal analysis formats.

Analysis of drug-protein binding by ultrafast affinity chromatography using immobilized human serum albumin.

Human serum albumin (HSA) was explored for use as a stationary phase and ligand in affinity microcolumns for the ultrafast extraction of free drug fractions and the use of this information for the analysis of drug-protein binding. Warfarin, imipramine, and ibuprofen were used as model analytes in this study. It was found that greater than 95% extraction of all these drugs could be achieved in as little as 250 ms on HSA microcolumns.

Analysis of lidocaine interactions with serum proteins using high-performance affinity chromatography.

High-performance affinity chromatography was used to study binding by the drug lidocaine to human serum albumin (HSA) and alpha(1)-acid glycoprotein (AGP). AGP had strong binding to lidocaine, with an association equilibrium constant (K(a)) of 1.1-1.

Evaluation of silica monoliths in affinity microcolumns for high-throughput analysis of drug-protein interactions.

Silica monoliths in affinity microcolumns were tested for the high-throughput analysis of drug-protein interactions. HSA was used as a model protein for this work, while carbamazepine and R-warfarin were used as model analytes. A comparison of HSA silica monoliths of various lengths indicated columns as short as 1 to 3 mm could be used to provide reproducible estimates of retention factors or plate heights.

Studies of imipramine binding to human serum albumin by high-performance affinity chromatography.

Binding by the drug imipramine to the protein human serum albumin (HSA) was studied by using high-performance affinity chromatography. The association equilibrium constants and number of binding sites for imipramine with HSA were first estimated by utilizing frontal analysis. Imipramine was found to have one major binding site on HSA with an association equilibrium constant of 1.

Characterization of drug-protein interactions in blood using high-performance affinity chromatography.

The binding of drugs with proteins in blood, serum, or plasma is an important process in determining the activity, distribution, rate of excretion, and toxicity of drugs in the body. High-performance affinity chromatography (HPAC) has received a great deal of interest as a means for studying these interactions. This review examines the various techniques that have been used in HPAC to examine drug-protein binding and discusses the types of information that can be obtained through this approach.

Studies of verapamil binding to human serum albumin by high-performance affinity chromatography.

The binding of verapamil to the protein human serum albumin (HSA) was examined by using high-performance affinity chromatography. Many previous reports have investigated the binding of verapamil with HSA, but the exact strength and nature of this interaction (e.g.