The European Genome-phenome Archive (EGA - https://ega-archive.org/) is a resource for long term secure archiving of all types of potentially identifiable genetic, phenotypic, and clinical data resulting from biomedical research projects. Its mission is to foster hosted data reuse, enable reproducibility, and accelerate biomedical and translational research in line with the FAIR principles. Launched in 2008, the EGA has grown quickly, currently archiving over 4,500 studies from nearly one thousand institutions. The EGA operates a distributed data access model in which requests are made to the data controller, not to the EGA, therefore, the submitter keeps control on who has access to the data and under which conditions. Given the size and value of data hosted, the EGA is constantly improving its value chain, that is, how the EGA can contribute to enhancing the value of human health data by facilitating its submission, discovery, access, and distribution, as well as leading the design and implementation of standards and methods necessary to deliver the value chain. The EGA has become a key GA4GH Driver Project, leading multiple development efforts and implementing new standards and tools, and has been appointed as an ELIXIR Core Data Resource.

No abstract

Meat color is an important aspect of consumer’spurchase decisions regarding meat products. Perceived meat color results from the interaction of light, a detector(i.e. human eye), and numerous factors that are both intrinsic and extrinsic tothe muscle which influence the chemical state of myoglobin.  The complex nature of these interactions dictatesthat decisions regarding evaluations of meat color be made carefully, and thatinvestigators have a basic knowledge of the physical and chemical factorsaffecting their evaluations.  Theseguidelines were compiled to aid investigators in navigating the pitfalls ofmeat color evaluation and ensure the reporting of information needed forappropriate interpretation of the resulting data.  The guidelines provide an overview ofmyoglobin chemistry, the perception of meat color, in addition to details ofinstrumentation used in meat color evaluation. Moreover, these guidelines detail practical considerations for simulatedretail display studies and provide details of the most common laboratorytechniques used in meat color literature. Importantly, the guidelines indicate the information that should beincluded when reporting meat color research to aid in appropriateinterpretation.  Practical considerationsneeded for troubleshooting meat color problems in a commercial setting areincluded as well.  Investigators areencouraged to review the entire guidelines before designing and conducting meatcolor research.

No abstract

No abstract

This study reports the reduction of metmyoglobin (MMb) via oxidation of malate to oxaloacetate and the regeneration of reduced nicotinamide adenine dinucleotide (NADH) via malate dehydrogenase (MDH). Two experiments were conducted to evaluate a malate-MDH-NADH system as a possible mechanism for MMb reduction. In experiment 1, kinetics of MDH and MMb reduction were determined, and the results showed that increasing concentrations of oxidized nicotinamide adenine dinucleotide (NAD(+)) and l-malate also increased (p < 0.05) MMb reduction in vitro. Experiment 2 assessed the reducing activity of beef muscle extracts with different concentrations of malate and NAD(+) added. Reduction of MMb in the muscle extracts via MDH was NAD(+), malate, and extract concentration dependent (p < 0.05). A new mechanism is described for the nonspecific and specific enzymatic reduction of MMb, which supports the hypothesis that malate can replenish NADH via MDH activity in post-mortem muscle, ultimately resulting in a more functional meat color.

No abstract

The purpose of this study was to assess the ability of mitochondrial and cytoplasmic malate dehydrogenase present in postrigor bovine skeletal muscle to use malate as a substrate for reduced nicotinamide adenine dinucleotide (NADH) regeneration and metmyoglobin (MMb) reduction via the malate-NAD(+)-MMb system. Furthermore, addition of lactate to beef mitochondrial and cytoplasmic isolates was evaluated to determine whether interactions between malate and lactate increased MMb reduction. Addition of malate to isolated beef mitochondrial and cytoplasmic isolates at pH 7.2 increased (p < 0.05) MMb reduction. MMb reduction resulting from addition of malate and lactate was equal to or greater than MMb reduction resulting from malate alone. This suggests that a combination of mitochondrial (malate) and cytoplasmic (lactate) factors can be used to regenerate the post-mortem pool of NADH, resulting in metmyoglobin reduction and meat color stabilization.