Amino Acids are the building blocks from which the body creates proteins. Twenty different amino acids are needed by the body to create the various proteins needed for growth and repair. Max Amino 1200 is a concentrated source of amino acids for use during periods of intense physical activity or stress. It contains a blend of free-form and di- and tri-peptide amino acids.

L-arginine is a substance that's found in nuts, fish, red meat, soy, whole grains, beans and dairy products. It's also available in supplements.

Some people take L-arginine because it's believed to relax and open your arteries, which might help lower blood pressure.

Studies on L-arginine have had mixed results. The most recent research suggests that L-arginine may lower blood pressure. However, larger studies need to be done to confirm that L-arginine supplements can reduce blood pressure before experts can recommend everyday use of these supplements.

Your body usually makes all the L-arginine it needs. Taking a supplement is rarely necessary and may be of benefit only to people who have a deficiency or an underlying health condition, such as diabetes.

 

Amino acids essential for the synthesis of structural proteins,enzymes, and some hormones and neurotransmitters. Amino acids are also involved in numerous metabolic pathways that affect exercise metabolism. Consequently, it has been suggested that athletes involved in intense training require additional protein in the dietor that they should supplement their diet with specific amino acids. I review here the rationale and the evidence for the potential ergogenic effect of short-term supplementation with protein and amino acids and the evidence for the potential anabolic effect of longer-term use when supplementation is combined with training. Ideal first with protein, then with the amino acids under the following headings: the potentially anabolic amino acids; the branched-chain amino acids, which have a somewhat different role in metabolism and in their potential effect on performance; glutamine,which is in a class of its own for its effects on the immune system; creatine, an amino acid that is not one of the building blocks of protein but is involved in short-term energy production in muscle;and hydroxymethylbutyrate (HMB), a potentially anabolic metabolite of the amino acid leucine.

 

Researchers have expended a considerable amount of effort on evaluating the effects of supplementation of branched-chain amino acids (BCAAs: leucine, isoleucine, and valine) on physiological and psychological responses to exercise (Blomstrandet al., 1991; Kreider, 1998; Wagenmakers,1998). There are two primary hypotheses regarding the ergogenic value of supplementation with these amino acids.

First, BCAA supplementation has been reported to decrease exercise-induced protein degradation and/or muscle enzyme release (an indicator of muscle damage) possibly by promoting an anti-catabolic hormonal profile (Carli et al., 1992;Coombes and McNaughton, 1995). Theoretically, BCAA supplementation during intense training may help minimize protein degradation and thereby lead to greater gains in fat-free mass. Although several studies support this hypothesis, additional research is necessary to determine the long-term effects of BCAA supplementation during training on markers of catabolism, body composition, and strength (Kreider,1998).

Second, the availability of BCAA during exercise has been theorized to contribute to central fatigue (Newsholmeet al., 1991). During endurance exercise, BCAAs are taken up by the muscles rather than the liver in order to contribute to oxidative metabolism. The source of BCAAs for muscular oxidative metabolism during exercise is the plasma BCAA pool, which is replenished through the catabolism of whole body proteins during endurance exercise (Davis, 1995; Kreider,1998; Newsholme et al., 1991). However, the oxidation of BCAAs in the muscle during prolonged exercise may exceed the catabolic capacity to increase BCAA availability, so plasma BCAA concentration may decline during prolonged endurance exercise (Blomstrand etal., 1988; Blomstrand et al., 1991). The decline in plasma BCAAs during endurance exercise can result in an increase in the ratio of free tryptophan to BCAAs. Free tryptophan and BCAAs compete for entry into the brain via the same amino-acid carrier (Newsholme et al., 1991). Therefore, a decrease in BCAAs in the blood facilitates entry of tryptophan into the brain. Moreover, most tryptophan in the blood is bound to albumin, and the proportion of tryptophan bound to albuminis influenced by the availability of long-chained fatty acids(Davis et al., 1992; Newsholmeet al., 1991). In endurance exercise free fatty-acid concentration rises, so the amount of tryptophan bound to albuminfalls, increasing the concentration of free tryptophan in the blood(Davis, 1995).