The CAS they reference is for alpha-methylsynephrine, otherwise known as Oxilofrine.

Oxilofrine is also pictured on the bottle.

Oxilofrine has a good oral bioavailability [1], decent half-life, good tolerability up to 120 mg +, and decently strong beta-adrenergic agonism [2].


[1] https://www.ncbi.nlm.nih.gov/pubmed/3403107
[2] https://www.ncbi.nlm.nih.gov/pubmed/3229871


The only question is whether or not oxilofrine is actually contained within the product. To my knowledge, oxilofrine does not exist naturally within the food supply. The "methylsynephrine" which is found in various cactii is "beta-O-methylsynephrine," otherwise known as beta-methoxy-synephrine. It should have little to no activity.

Glutamine serves as a gluconeogenic precursor when muscle glycogen is depleted by approximately 90%; however, resistance training typically produces approximately 40% depletion in muscle glycogen, which may not be severe enough to benefit from glutamine supplementation. Than again, 99.9% of the human population will never reach a state where it is necessitated. There is a vast amount of data to prove and conclude its ineffectiveness.

With the exception of supplemental glutamine's beneficial role in gastrointestinal disorders (and general gut health), sepsis, and for the recovery from trauma and or surgery.... there's not much sense in administering a product that is very much limited in it's availability for physiological uptake, due to the fact that it's endogenous levels (prior to supplementation) are double the concentration of any other amino acid within the human body (1). Additionally, free form glutamine is unstable in solution at physiological pH.

_________________________________________________________________________________________________________

Facts and fallacies of purported ergogenic amino acid supplements.

Williams MH.

Department of Exercise Science, Physical Education, and Recreation, Old Dominion University, Norfolk, Virginia, USA. mwilliam@odu.edu

Although current research suggests that individuals involved in either high-intensity resistance or endurance exercise may have an increased need for dietary protein, the available research is either equivocal or negative relative to the ergogenic effects of supplementation with individual amino acids. Although some research suggests that the induction of hyperaminoacidemia via intravenous infusion of a balanced amino acid mixture may induce an increased muscle protein synthesis after exercise, no data support the finding that oral supplementation with amino acids, in contrast to dietary protein, as the source of amino acids is more effective. Some well-controlled studies suggest that aspartate salt supplementation may enhance endurance performance, but other studies do not, meriting additional research. Current data, including results for several well-controlled studies, indicated that supplementation with arginine, ornithine, or lysine, either separately or in combination, does not enhance the effect of exercise stimulation on either hGH or various measures of muscular strength or power in experienced weightlifters. Plasma levels of BCAA and tryptophan may play important roles in the cause of central fatigue during exercise, but the effects of BCAA or tryptophan supplementation do not seem to be effective ergogenics for endurance exercise performance, particularly when compared with carbohydrate supplementation, a more natural choice. Although glutamine supplementation may increase plasma glutamine levels, its effect on enhancement of the immune system and prevention of adverse effects of the overtraining syndrome are equivocal. Glycine, a precursor for creatine, does not seem to possess the ergogenic potential of creatine supplementation. Research with metabolic by-products of amino acid metabolism is in its infancy, and current research findings are equivocal relative to ergogenic applications. In general, physically active individuals are advised to obtain necessary amino acids through consumption of natural, high-quality protein foods.

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Glutamine: commercially essential or conditionally essential? A critical appraisal of the human data.

Am J Clin Nutr. 2001 Jul;74(1):25-32. Buchman AL.
Division of Gastroenterology and Hepatology, Northwestern University, Chicago, IL 60611, USA. a-buchman@nwu.edu

Glutamine is a nonessential amino acid that can be synthesized from glutamate and glutamic acid by glutamate-ammonia ligase. Glutamine is an important fuel source for the small intestine. It was proposed that glutamine is necessary for the maintenance of normal intestinal morphology and function in the absence of luminal nutrients. However, intestinal morphologic and functional changes related to enteral fasting and parenteral nutrition are less significant in humans than in animal models and may not be clinically significant. Therefore, it is unclear whether glutamine is necessary for the preservation of normal intestinal morphology and function in humans during parenteral nutrition. It was suggested that both glutamine-supplemented parenteral nutrition and enteral diets may pre-vent bacterial translocation via the preservation and augmentation of small bowel villus morphology, intestinal permeability, and intestinal immune function. However, it is unclear whether clinically relevant bacterial translocation even occurs in humans, much less whether there is any value in the prevention of such occurrences. Results of the therapeutic use of glutamine in humans at nonphysiologic doses indicate limited efficacy. Although glutamine is generally recognized to be safe on the basis of relatively small studies, side effects in patients receiving home parenteral nutrition and in those with liver-function abnormalities have been described. Therefore, on the basis of currently available clinical data, it is inappropriate to recommend glutamine for therapeutic use in any condition.

________________________________________________________

Effect of glutamine supplementation combined with resistance training in young adults.

Candow DG, Chilibeck PD, Burke DG, Davison KS, Smith-Palmer T.

College of Kinesiology, University of Saskatchewan, Saskatoon, Canada.

The purpose of this study was to assess the effect of oral glutamine supplementation combined with resistance training in young adults. A group of 31 subjects, aged 18-24 years, were randomly allocated to groups (double blind) to receive either glutamine (0.9 g x kg lean tissue mass(-1) x day(-1); n = 17) or a placebo (0.9 g maltodextrin x kg lean tissue mass(-1) x day(-1); n = 14 during 6 weeks of total body resistance training. Exercises were performed for four to five sets of 6-12 repetitions at intensities ranging from 60% to 90% 1 repetition maximum (1 RM). Before and after training, measurements were taken of 1 RM squat and bench press strength, peak knee extension torque (using an isokinetic dynamometer), lean tissue mass (dual energy X-ray absorptiometry) and muscle protein degradation (urinary 3-methylhistidine by high performance liquid chromatography). Repeated measures ANOVA showed that strength, torque, lean tissue mass and 3-methylhistidine increased with training (P < 0.05), with no significant difference between groups. Both groups increased their 1 RM squat by approximately 30% and 1 RM bench press by approximately 14%. The glutamine group showed increases of 6% for knee extension torque, 2% for lean tissue mass and 41% for urinary levels of 3-methylhistidine. The placebo group increased knee extension torque by 5%, lean tissue mass by 1.7% and 3-methylhistidine by 56%. We conclude that glutamine supplementation during resistance training has no significant effect on muscle performance, body composition or muscle protein degradation in young healthy adults.

_____________________________________________________________________________________________

Exercise-induced immunodepression- plasma glutamine is not the link.

Hiscock N, Pedersen BK.

Copenhagen Muscle Research Centre and Department of Infectious Diseases, Rigshospitalet, University of Copenhagen, DK-2100 Copenhagen, Denmark.

The amino acid glutamine is known to be important for the function of some immune cells in vitro. It has been proposed that the decrease in plasma glutamine concentration in relation to catabolic conditions, including prolonged, exhaustive exercise, results in a lack of glutamine for these cells and may be responsible for the transient immunodepression commonly observed after acute, exhaustive exercise. It has been unclear, however, whether the magnitude of the observed decrease in plasma glutamine concentration would be great enough to compromise the function of immune cells. In fact, intracellular glutamine concentration may not be compromised when plasma levels are decreased postexercise. In addition, a number of recent intervention studies with glutamine feeding demonstrate that, although the plasma concentration of glutamine is kept constant during and after acute, strenuous exercise, glutamine supplementation does not abolish the postexercise decrease in in vitro cellular immunity, including low lymphocyte number, impaired lymphocyte proliferation, impaired natural killer and lymphokine-activated killer cell activity, as well as low production rate and concentration of salivary IgA. It is concluded that, although the glutamine hypothesis may explain immunodepression related to other stressful conditions such as trauma and burn, plasma glutamine concentration is not likely to play a mechanistic role in exercise-induced immunodepression.

__________________________________________________________________________________________

Addition of glutamine to essential amino acids and carbohydrate does not enhance anabolism in young human males following exercise.

Wilkinson SB, Kim PL, Armstrong D, Phillips SM.

Exercise Metabolism Research Group, Department of Kinesiology, McMaster University, 1280 Main St. West, Hamilton, ON L8S 4K1, Canada.

We examined the effect of a post-exercise oral carbohydrate (CHO, 1 g.kg(-1).h(-1)) and essential amino acid (EAA, 9.25 g) solution containing glutamine (0.3 g/kg BW; GLN trial) versus an isoenergetic CHO-EAA solution without glutamine (control, CON trial) on muscle glycogen resynthesis and whole-body protein turnover following 90 min of cycling at 65% VO2 peak. Over the course of 3 h of recovery, muscle biopsies were taken to measure glycogen resynthesis and mixed muscle protein synthesis (MPS), by incorporation of [ring-2H5] phenylalanine. Infusion of [1-13C] leucine was used to measure whole-body protein turnover. Exercise resulted in a significant decrease in muscle glycogen (p < 0.05) with similar declines in each trial. Glycogen resynthesis following 3 h of recovery indicated no difference in total accumulation or rate of repletion. Leucine oxidation increased 2.5 fold (p < 0.05) during exercise, returned to resting levels immediately post-exercise,and was again elevated at 3 h post-exercise (p < 0.05). Leucine flux, an index of whole-body protein breakdown rate, was reduced during exercise, but increased to resting levels immediately post-exercise, and was further increased at 3 h post-exercise (p < 0.05), but only during the CON trial. Exercise resulted in a marked suppression of whole-body protein synthesis (50% of rest; p < 0.05), which was restored post-exercise; however, the addition of glutamine did not affect whole-body protein synthesis post-exercise. The rate of MPS was not different between trials. The addition of glutamine to a CHO + EAA beverage had no effect on post-exercise muscle glycogen resynthesis or muscle protein synthesis, but may suppress a rise in whole-body proteolysis during the later stages of recovery.

PMID: 17111006 [PubMed - indexed for MEDLINE]

________________________________________________________________________________

Amino acids and endurance exercise.

Hargreaves MH, Snow R.

School of Health Sciences, Deakin University, Burwood, 3125, Australia.

Although skeletal muscle is capable of oxidizing selected amino acids, exercise in the fed and carbohydrate-replete condition results in only a small increase in amino acid utilization. Nevertheless, it may be important to increase the dietary protein requirements of active individuals. There is ongoing debate as to whether the amino acids for oxidation are derived from the free amino acid pool, from net protein breakdown, or a combination of both. There has been interest in the potential ergogenic benefits of amino acid ingestion; however, BCAA ingestion does not appear to affect fatigue during prolonged exercise, there is little support from controlled studies to recommend glutamine ingestion for enhanced immune function, and although glutamine stimulates muscle glycogen synthesis, its addition to carbohydrate supplements provides no additional benefit over ingestion of carbohydrate alone.


PMID: 11255141 [PubMed - indexed for MEDLINE]

___________________________________________________________________________________________

The Effects of High-Dose Glutamine Ingestion on Weightlifting Performance

JOSE ANTONIO1, 3, MICHAEL S. SANDERS1, DOUGLAS KALMAN2, DEREK WOODGATE1, and CHRIS STREET1

1. Sports Science Laboratory, University of Delaware, Newark, Delaware 19716, 2. Peak Wellness, Greenwich, Connecticut 06830, 3. Address correspondence to Jose Antonio, Scientific Affairs Department, Nutricia, 6111 Broken Sound Parkway NW, Boca Raton, FL 33487

The purpose of this study was to determine if high-dose glutamine ingestion affected weightlifting performance. In a double-blind, placebo-controlled, crossover study, 6 resistance-trained men (mean ? SE: age, 21.5 ? 0.3 years; weight, 76.5 ? 2.8 kg−1) performed weightlifting exercises after the ingestion of glutamine or glycine (0.3 g?kg−1) mixed with calorie-free fruit juice or placebo (calorie-free fruit juice only). Each subject underwent each of the 3 treatments in a randomized order. One hour after ingestion, subjects performed 4 total sets of exercise to momentary muscular failure (2 sets of leg presses at 200% of body weight, 2 sets of bench presses at 100% of body weight). There were no differences in the average number of maximal repetitions performed in the leg press or bench press exercises among the 3 groups. These data indicate that the short-term ingestion of glutamine does not enhance weightlifting performance in resistance-trained men.

Reference Data:Antonio, J., M.S. Sanders, D. Kalman, D. Woodgate, and C. Street. The effects of high-dose glutamine ingestion on weightlifting performance.

Keywords: amino acid, supplement, nutrition, protein

DOI: 10.1519/1533-4287(2002)016[0157:TEOHDG]2.0.CO;2

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Clin Nutr. 1996 Oct ;15 (5):267-73 16844055

Effect of a short-term infusion of glutamine on muscle protein metabolism postoperatively.

[My paper] A Januszkiewicz , P Ess?n , M A McNurlan , G A Calder , K Andersson , J Wernerman , P J Garlick

The acute effect of a short-term postoperative infusion of glucose supplemented withglutamine (0.285 g/kg body weight), on muscle protein metabolism, was studied by analyses of free amino acid concentrations and determinations of protein synthesis. A glutamine-glucose infusion was given for 5.5 h to 6 patients 2-3 days after elective surgery for colon cancer. The free glutamine concentration was 5.72 +/- 0.96 mmol/kg wet weight (ww) before and 6.14 +/- 1.10 mmol/kg ww 4 h after the glutamine infusion. The rate of protein synthesis was 1.26 +/- 0.15%/24 h before the infusion and 1.12 +/- 0.16%/24 h during its latter part. The percentage of polyribosomes was 42.2 +/- 3.4% before and 40.9 +/- 1.3% after the infusion. The results showed no difference in these biochemical parameters, indicating that a short-term infusion of glutamine given postoperatively is insufficient to affect protein metabolism in human skeletal muscle.

Vascular effects of prostacyclin: does activation of PPARδ play a role?
Katusic ZS, Santhanam AV, He T.
SourceDepartments of Anesthesiology, Molecular Pharmacology and Experimental Therapeutics, Mayo Clinic College of Medicine, Rochester, MN, USA.

Abstract
Prostacyclin (PGI(2)) is a potent vasodilator that exerts multiple vasoprotective effects in the cardiovascular system. The effects of PGI(2) are mediated by activation of the cell membrane G-protein-coupled PGI(2) receptor (IP receptor). More recently, however, it has been suggested that PGI(2) might also serve as an endogenous ligand and activator of nuclear peroxisome proliferator-activated receptorδ (PPARδ). Consistent with this concept, studies designed to define pharmacological properties of stable PGI(2) analogs revealed that beneficial effects of these compounds appear to be mediated, in part, by activation of PPARδ. This review discusses emerging evidence regarding the contribution of PPARδ activation to vasoprotective and regenerative functions of PGI(2) and stable analogs of PGI(2).

Part of the reason could very well be the fact taurine acts as an osmolyte and exercise can deplete it to varying degrees. While you can't acheive superphysiological levels of taurine as shown in Galloway 2008 you can certainly offset it's depletion while training through supplementing it before or during training.

In general though, I do think it helps maintain electrolyte balance and fluid balance as shown by Narada 2004 which could help in endurance leves and even increasing force contraction potential alluded to an in vitro study by Goodman 2009. All of these factors added up definitely point to the efficacy of taurine supplementation and back-up the in vivo results in humans shown by Zhang 2004 which showed oral taurine attenuated exercise induced DNA damage and increased exercise capacity in cyclists.

Yatabe Y, Miyakawa S, Ohmori H, Mishima H, Adachi T. Effects of taurine administration on exercise. Adv Exp Med Biol. 2009;643:245-52.

Taurine concentration in rat skeletal muscles after endurance running, with and without taurine administration was studied. Taurine concentrations in skeletal muscles was significantly decreased in exercised groups without taurine administration. However, taurine administration reduced the decrease of taurine concentration in skeletal muscles in exercise. Oral administration of taurine has effect for maintaining taurine concentration in skeletal muscles in exercise. The duration of running time to exhaustion of rats, with and without taurine administration were studied. The duration of running time to exhaustion was significantly increased by taurine administration. Oral administration of taurine increases the ability of physical endurance. Rat urinary excretions of creatinine, creatine, 3-methylhistidine (3-MH) after treadmill running, with and without taurine administration were studied. Rat urinary excretions of creatinine, creatine, 3-MH after treadmill running was significantly decreased with taurine administration. Taurine administration was considered to reduce the exercise-induced muscle fatigue.

Peroxisome proliferator-activated delta (PPARδ ) control the transcription of genes involved in lipid metabolism. Activation of PPARδ may have antiatherogenic effects through the increase of plasma HDL, theoretically promoting reverse cholesterol transport from peripheral tissues toward the liver for removal via bile and feces. Effects of PPARδ activation by agonist GW1516 has been demonstrated to effectively reverse metabolic abnormalities in obese men with metabolic syndrome (a pre-diabetic condition), likely due to the fact that it stimulus fatty acid oxidation.

GW1516 holds promise for treating obesity and adiposity and has been touted, much like AICAR, as "exercise in a pill," etc. In conjunction with AICAR, an AMPK agonist which acts synergistically with GW1516, significant increases in exercise endurance have been demonstrated in animal studies.

GW1516 and AICAR are becoming popular items in the bodybuilding grey market. My approach here is try to mimic the effects of the combo termed exercise in a pill using supplement available in the market. Here are some of of the substances that can potentially work in a similar manner:

Potential PPARδ agonist or activators (GW1516 mimcers):


1) Tetradecylthioacetic acid (TTA): TTA is a non-selective PPAR agonist similar to GW1516 it activates PPARδ (weaker/less affinity) All three rodent peroxisome proliferator-activated receptor (PPAR) subtypes were activated by TTA in the ranking order PPARalpha > PPARdelta > PPARgamma. TTA is a non-beta-oxidizable fatty acid analog, which potently regulates lipid homeostasis.


2) Arachidonic acid (AA): PPARs are activated by their ligands, among which are arachidonic acid and other PUFAs (polyunsaturated fatty acids) , NSAIDs and cyclopentenone PGs. There are at least three PPARs, PPARα, PPARδ and PPARγ, of which the PPARα and PPARδ isoforms. Therefore activation of a PPAR is one mechanism by which arachidonic acid may induce PTGS2.
3) Sessamin and fish oil: Sesamin acts primarily as a ppar-agonist of the alpha type, but there is evidence that it maybe a weak activator of of other PPAR subtypes

Potential AMPK agonist (AICAR mimcers):

1) Forskolin: Is unique in its ability to stimulate adenylate cyclase activity and increasec AMP which regulates and activates critical enzymes required for the cellular energy. Long-term forskolin stimulation induces AMPK activation similar to AICAR
2) Methylxanthines: It is a competitive nonselective phosphodiesterase inhibitors which raise intracellular cAMP, activate PKA, inhibit TNF-alpha and leukotriene This is found in CL popular supplement White flood.


Other potential candidates: berberine, Caffiene, Alisma plantago aquatica (ze xie/european waterplantain), Catharanthus roseus (madagascar periwinkle), Acorus calamus (sweet calamus), Euphorbia balsamifera (balsam spurge), Jatropha curcas (barbados nut), Origanum majorana (marjoram), Zea mays (corn silk), Capsicum frutescens (chilli) and Urtica dioica (stinging nettle).

For the past year, researchers have been going back and forth debating which was more anabolic…whey protein or essential amino acids (EAAs). A few months ago, it seemed that EAA was the winner; in a previous study, researchers administered either 15 grams of whey protein or 15 grams of EAA to elderly participants. They found that ingestion of 15 grams of EAA more than doubles muscle protein balance in elderly persons when compared to that of the ingestion of 15 grams of whey, which would support a greater importance of the EAA (as opposed to whey) in improving muscle protein synthesis in elderly persons. EAA seemed like the more anabolic supplement, but the researchers went back and examined the data and found that 15 grams of whey protein contained only 7 grams of EAA! So, the study did not have the exact same EAA mix for whey protein compared to the EAA mix (7 grams of EAA found in whey compared to 15 grams of EAA).

The same research group went back and administered a dose-to-dose comparison and administered 15 grams of whey, which contains roughly 7 grams of EAA and compared it to an equivalent EAA dose (~6.72 grams of EAA). To the researchers’ surprise, whey protein resulted in greater anabolic effects than EAA when compared dose per dose. The study reported that EAAs are not solely responsible for the anabolic properties of whey protein. The researchers concluded that whey protein (whole consumption) is greater than the sum of its parts (EAA), or effects beyond that of just the amino acid content. So what ingredient in whey protein could be enhancing anabolic actions? It is interesting that the two dosages each had the exact same dosage of leucine, so there was something else in whey protein causing the greater anabolic effect. The researchers hypothesized that the increase in the plasma concentration of the amino acid cysteine from whey protein, which has previously been found to augment muscle protein anabolism, may have enhanced muscle protein synthesis. Whey protein resulted in a greater insulin response than EAA, which also could have augmented the anabolic actions of whey protein. The researchers explained that whey protein is a potent stimulator of Gastric Inhibitory Polypeptide (GIP), also known as the glucose-dependent insulinotropic peptide. It is now believed that the function of GIP is to induce insulin secretion. Relative to that, it is known that whey protein is a strong stimulator of GIP secretagogue, possibly through bioactive peptides present in whey or formed during its digestion, and that the plasma GIP concentration is greater after ingestion of intact protein than a similar amount of protein in the form of free amino acids. The researchers also commented that whey protein is inexpensive and also has additional health benefits that can’t be found in EAA. For example, cysteine-supported glutathione synthesis is implicated in protection against oxidative stress, whereas beta-lactoglobulin and alpha-lactalbumin are major whey proteins modulating immune function. The researchers concluded that the anabolic actions of whey go beyond just EAAs and the whole (whey protein) are greater than the sum of parts (EAA).

When I first started researching NMDA, I was considering marketing it as a nutritional supplement. After delving in deeper however, a couple of things made me change my mind. First of all, I contacted the patent inventor to see if I could get some more information on NMDA. He regretfully told me that his later research failed to confirm his earlier findings, and that he had deemed the project not worthy of further pursuit. I also discovered that NMDA is potentially quite toxic and may destroy neurons in sensitive areas of the brain like the hippocampus and the basal ganglia. NMDA might also have the capacity to induce convulsions in susceptible individuals.

So what, if any, lesson was learned from this dead end research endeavor? Well, I did receive a clear reminder never to jump to conclusions based upon limited evidence – particularly never to make assumptions based solely upon patent information (which is not subject to peer review and is notoriously inaccurate). If only the marketers of the “flavor of the month” supplement 5-methyl-7-methoxy-isoflavone would have heeded such advice; perhaps consumers would have been saved from what is, in my opinion, yet another supplement disappointment.

-PA

Originally Posted by Diesel0022

R1- Lets keep this thread clean of personal dislikes and on topic.

What is your input on Soy Protein raising estrogen? I've read that the process of which soy protein is extracted uses alcohol, which depletes more than 98% of phyto-estrogen content.

"You know the fun thing about the soy protein debate is people only hear what they want to hear, yes soy protein contains phyto-estrogen base which does highly mimic the properties of human estrogen, but the strange thing is under low doses phyto estrogen actually attaches itself to human estrogen cells making the body believe there is more estrogen in the body so it actually lowers it's estrogen production to comphensate, yet phyto estrogen doesn't have all the catabolic properties as normal human estrogen."

It seems to be a torn discussion. There are studies proving both sides. I personally think it does not affect hormones to any measurable degree. Any insight on the subject is appreciated

Both sides of the argument so read carefully.

 

 

Originally Posted by D3Baseball

The point is that based on available research, soy protein isolate should be considered a viable choice for protein supplementation.

There is a chance, I'll admit, that a complete dietary replacement of chicken, beef, milk, fish proteins in favor of soy could make a small, imperceptible difference in hormone profiles. I'd say this effect, while perhaps unlikely, has not been definitively ruled out just yet.

What we're arguing about, though, is supplementation. Will 30-60g per day of SPI-90 hurt your gains/make you unhealthy? I just don't think so, and I hope Pat can shed some light on this. This is a particularly relevant question because whey protein is getting damn expensive and SPI-90 offers a decent taste, nice nutrition profile, and cheap alternative.

 

 

 

Originally Posted by Patrick Arnold

i was talking to douglas kalman recently who said that he studied a group of males ingesting soy protein powder (a substantial amount per day) and after a period of time they showed no disturbance in hormone levels

i think soy protein powder is ok but i would limit it to 30 -40 grams a day still just to be safe

 

 

 

Originally Posted by Diesel0022

Do you know how much was being ingested during that study? Is it/will it be published?

 

 

 

Originally Posted by Patrick Arnold

i dont remember but he may have said 60g

i dunno whether it will be published. i didnt pursue the line of conversatoin

 

 

 

Originally Posted by T-Bone

The Soy hysteria on this board is laughable. I remember a thread where a guy was going to the supermarket and looking through every single brand of tuna to find one that had no trace amounts of soy. He was thinking the soy in the tuna was going to make him grow boobs.

 

 

 

 

Originally Posted by Diesel0022

So since most get that amount from shakes per day, personally I do 2 shakes when needed which is 40gPRO, would you agree that soy protein supplementation is safe in regards to null effects on hormones and is a viable option?



Its out of control, soy doesn't give you man boobs. ****ty genetics do.

 

 

 

Originally Posted by Tmac29

Yea there are a few on bb.com that LOOOOOVE to quickly say that Soy = the man boobies.

 

 

 

Originally Posted by D3Baseball

I'd be more interested in a comparison to casein or egg.

 

 

 

Originally Posted by D3Baseball

This train of thought is about as popular as "eat frequent meals" in the United States

 

 

 

Originally Posted by Patrick Arnold

probably.

there are other soy products which are much more rich in isoflavones than soy protein isolate

Effects of beta-alanine supplementation on sprint endurance.
Jagim AR, Wright GA, Brice AG, Doberstein ST.
SourceExercise & Sport Science1, Biology Dept2, UW-La Crosse, La Crosse, WI.

Abstract
PURPOSE: Recent research has shown that beta-alanine supplementation can increase intramuscular carnosine levels. Carnosine is an intramuscular buffer and has been linked to improvements in performance, specifically during bouts of high intensity exercise that are likely limited by muscle acidosis. Therefore the purpose of this study was to examine the effect of beta-alanine supplementation (BA) on sprint endurance at two different supramaximal intensities.

METHODS: Twenty-one anaerobically trained [rugby players (n=4), wrestlers (n=11) and recreationally strength-trained athletes (n=6)] college men participated in a double blind, placebo controlled study. Subjects performed an incremental VO2 max test and two sprint to exhaustion tests set at 115% and 140% of their VO2 max on a motorized treadmill before (PRE) and after (POST) a 5 week supplementation period. During this time subjects ingested either a BA supplement or placebo (PLA) with meals. Subjects ingested 4g /day of BA or PLA during the first week and 6g/day the following 4 weeks. Capillary blood samples were taken before and after each sprint to determine blood lactate response to the sprint exercise RESULTS No significant group (BA, PLA) x intensity (115%, 140%; p=0.60), group by time (PRE, POST; p=0.72), or group x intensity x time (p=0.74) interactions were observed for time to exhaustion (See Table 1). In addition, similar non-significant observations were made for lactate response to the sprints (group x intensity, p=0.43; group x time, p=0.33, group x intensity x time, p=0.56)

CONCLUSION: From the results of the current study, it was concluded that beta-alanine supplementation did not have a significant effect on sprint endurance at supramaximal intensities.