Acute oral application of a magnesium amino acid compound: Significant improvement of individual performance in sports

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Abstract

Abstract. Seventeen male officer trainees (between 20 and 24 years of age) of the Theresan Military Academy in Wiener Neustadt (Austria) have been subjected to a standardized 2,400-m run as a fitness test. Before and after the run, capillary blood samples for determination of pH, pCO 2 , pO 2 , HCO 3, base excess (BE), ionized Mg, and lactate were drawn, and heart rate (HR) and RRsys were determined. On the next day, the subjects received two sachets of an effervescent compound (“Dr. Böhm Mg plus Aminosäuren”, Apomedica, Graz, Austria) in 125 mL of tap water, containing electrolytes (Mg 150 mg, K 180 mg), trace elements (Zn 5 mg, Se 25 µg), vitamins (vitamin C 50 mg, riboflavin 0.26 mg, niacin 8 mg, B6 1.4 mg, B 12 3 µg), amino-acids (leucine 600 mg, isoleucine 300 mg, valin 300 mg, argininaspartate 400 mg, l-carnitine 200 mg, taurine 200 mg), and herbal antioxidants (resveratrol 2 mg, green tea extract 25 mg) after blood sampling, and the same 2,400-m run as before was performed again with another consecutive sampling. It turned out that the drop in BE, pCO 2 , HCO 3 , and Mg due to the run was significantly smaller in the treatment group than in controls (p < 0.05). The increase in lactate and RRsys on the other hand was significantly higher in the control group (p < 0.05). Also, Mg changes due to the run were much less uniform in Mg-treated subjects. Linear correlations, which developed significantly between ionized Mg, pO 2 , pCO 2 , BE, and lactate, as well as significant linear correlations between heart rate and lactate, and also between Mg and running time (our performance marker), were in fact always seen in untreated subjects but never in Mg-treated participants. We deduce that acute Mg and amino acid application before sport enhances Mg availability for muscle-energy turnover, and at the same time, (enzyme) protein synthesis is enhanced. This creates an at least (vitamins and antioxidants are also applied) two-pronged useful effect on effort and performance. 

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Ingested protein dose response of muscle and albumin protein synthesis after resistance exercise in young men.

J. E. M. Robinson, Thomas Glover, Mark Tarnopolsky … (2008)

The anabolic effect of resistance exercise is enhanced by the provision of dietary protein. We aimed to determine the ingested protein dose response of muscle (MPS) and albumin protein synthesis (APS) after resistance exercise. In addition, we measured the phosphorylation of candidate signaling proteins thought to regulate acute changes in MPS. Six healthy young men reported to the laboratory on 5 separate occasions to perform an intense bout of leg-based resistance exercise. After exercise, participants consumed, in a randomized order, drinks containing 0, 5, 10, 20, or 40 g whole egg protein. Protein synthesis and whole-body leucine oxidation were measured over 4 h after exercise by a primed constant infusion of [1-(13)C]leucine. MPS displayed a dose response to dietary protein ingestion and was maximally stimulated at 20 g. The phosphorylation of ribosomal protein S6 kinase (Thr(389)), ribosomal protein S6 (Ser(240/244)), and the epsilon-subunit of eukaryotic initiation factor 2B (Ser(539)) were unaffected by protein ingestion. APS increased in a dose-dependent manner and also reached a plateau at 20 g ingested protein. Leucine oxidation was significantly increased after 20 and 40 g protein were ingested. Ingestion of 20 g intact protein is sufficient to maximally stimulate MPS and APS after resistance exercise. Phosphorylation of candidate signaling proteins was not enhanced with any dose of protein ingested, which suggested that the stimulation of MPS after resistance exercise may be related to amino acid availability. Finally, dietary protein consumed after exercise in excess of the rate at which it can be incorporated into tissue protein stimulates irreversible oxidation.

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Leucine-enriched essential amino acid supplementation during moderate steady state exercise enhances postexercise muscle protein synthesis.

Lee Margolis, Janet A. Young, James McClung … (2011)

The effects of essential amino acid (EAA) supplementation during moderate steady state (ie, endurance) exercise on postexercise skeletal muscle metabolism are not well described, and the potential role of supplemental leucine on muscle protein synthesis (MPS) and associated molecular responses remains to be elucidated. This randomized crossover study examined whether EAA supplementation with 2 different concentrations of leucine affected post-steady state exercise MPS, whole-body protein turnover, and mammalian target of rapamycin 1 (mTORC1) intracellular signaling. Eight adults completed 2 separate bouts of cycle ergometry [60 min, 60% VO(2)peak (peak oxygen uptake)]. Isonitrogenous (10 g EAA) drinks with different leucine contents [leucine-enriched (l)-EAA, 3.5 g leucine; EAA, 1.87 g leucine] were consumed during exercise. MPS and whole-body protein turnover were determined by using primed continuous infusions of [(2)H(5)]phenylalanine and [1-(13)C]leucine. Multiplex and immunoblot analyses were used to quantify mTORC1 signaling. MPS was 33% greater (P < 0.05) after consumption of L-EAA (0.08 ± 0.01%/h) than after consumption of EAA (0.06 ± 0.01%/h). Whole-body protein breakdown and synthesis were lower (P < 0.05) and oxidation was greater (P < 0.05) after consumption of L-EAA than after consumption of EAA. Regardless of dietary treatment, multiplex analysis indicated that Akt and mammalian target of rapamycin phosphorylation were increased (P < 0.05) 30 min after exercise. Immunoblot analysis indicated that phosphorylation of ribosomal protein S6 and extracellular-signal regulated protein kinase increased (P < 0.05) and phosphorylation of eukaryotic elongation factor 2 decreased (P < 0.05) after exercise but was not affected by dietary treatment. These findings suggest that increasing the concentration of leucine in an EAA supplement consumed during steady state exercise elicits a greater MPS response during recovery. This trial is registered at clinicaltrials.gov as NCT01366924.

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Molecular mechanism of Mg-ATPase activity.

Eka Nozadze, Nana Arutinova, Leila Tsakadze … (2015)

Mg-ATPase is very important in living organisms. To better understand the molecular mechanism of Mg-ATPase activity, we applied the method of kinetic analysis of multi-sited enzyme systems; this is a suitable approach used for kinetic investigation of multi-sited enzyme systems. The study of Mg-ATPase has demonstrated: (1) It is a multi-sited enzyme system whose functional unit is minimum a dimmer; (2) Its substrate is MgATP, while free ATP and Mg(2+) appear to be the enzyme modifiers with a dual effect; (3) The enzyme system for MgATP has at least three sites: i.e., the essential activator, full inhibitor, and partial effect modifiers sites; (4) Mg-ATPase carries out Mg(2+) transport through the 1Mg(2+):1ATP stochiometry. Based on the results of these analyses, the kinetic scheme for Mg-ATPase has been developed.