10-16-2005, 11:36 PM #1
Question on amounts/type of carbs needed after workout
I would like to know what you guys think of dorian yates mbf, it has 42 grams of protien and 84 grams of carbs per serving, problem is I dont know how much is dextrose and how much is maltodextrin. I read you need like 80 to 100 grams with 50 percent of each, after post workout? Also is it a good idea to eat raisins after workout for simple sugars like fructose? If so, How many grams is good? Anyone have an opinion on vitargo? Also is it good to spike ur insulin after workout. I have heard different opinions. When should your insulin be spiked and what kind of foods beside simple sugars are good?
10-17-2005, 01:13 AM #2
PWO you should have a whey protein and dextrose/maltodextrin shake. The amounts are relavent to you body weight/goals/etc.... but twice as much dex/malto to whey is the correct ratio. Why eat raisins when you have dex or malto?
10-17-2005, 02:39 AM #3
so should you get a shake that already has that or on the side. which solid foods can u get dex/malto
10-17-2005, 03:01 AM #4
10-17-2005, 05:21 AM #5
but that varies in the amount of dex per different brand
i think most are 50/50 dex/fructose
i like to use a spoonful or 2 PWO along with regular DEx
there's no real harm in eating raisins PWO but dont rely on them for repleshing your glycogen stores (cos they wont)
10-17-2005, 11:16 AM #6
you can go with just straight dextrose. no need for the maltodextrin. for every one gram of dextrose there is one carb, 84g of dextrose= 84g of carbs
10-18-2005, 04:53 AM #7
I did not quite follow jdh, can anyone clarify what he means? So if I am talking mbf which has 84 grams of carbs per serving do i still need dex and malto
10-18-2005, 06:12 AM #8Originally Posted by superfat73
So finish the mbf, and then get some whey and dex and make your own PWO shake because it will be much cheaper and equally good.
10-18-2005, 10:13 PM #9
Let me know what you do..I'll do the same I need to get my pwo shakes and diet down
10-19-2005, 02:38 AM #10
when it comes to this you have 2 schools of thought.
One say a 50/50 blend betwen malto and dextro(or just plain dextro if you can stomach the sweetness) around 80-100grams imidietly post workout is the best way to do it. They say that quick glycogen replenishment is important for anabolic processes.
The other say that it doesnt matter what carb you use, milk, fruit, oatmeal. Anything will do and spiking insulin is unnessecary since imidiate quick glycogen replenishment has no importance on muscle tissue buildup.
I suggest you try both for a period of time and check what works best for you.
10-19-2005, 07:07 AM #11Originally Posted by johan
So Johan I heard of people just grabbing a soda and eating some fruit after their workout, since your second statment suggested any type of carb I guess this would work too? What's your take?
10-19-2005, 07:20 AM #12Originally Posted by 24labor
10-19-2005, 09:31 AM #13Originally Posted by 24labor
10-19-2005, 10:26 AM #14
how does immediate replenishment of glycogen NOT have an effect on building muscle? your muscle is primed for growth and repair after workout. it is without protein and carbs. thats the purpose of having a whey/dex drink after workout, to start the repair and building of muscle tissue. in order to do this you have to spike your insulin level in order to transport the building blocks to your muscles.
10-19-2005, 10:28 AM #15
10-19-2005, 10:33 AM #16Originally Posted by jdh
And not exogenous slin either becuase that isnt a factor in this case.
We all know exogenous slin is anabolic .
10-19-2005, 11:18 AM #17
i guess i stated it wrong. i didnt mean it to sound that it increases protein synthesis just that a spike in insulin is necessary to quickly replenish muscle glycogen stores and transporting nutrients to the cell as well. and being that your muscles are in need of that following a workout why would you not want that process to start as quick as possible. i dont believe for one second though that having high glycemic carbs pwo is going to lead toward the storage of body fat. i recently reduced my bf% by about 10% this past year. i ate low carb but consumed 100 grams of dextrose with whey for my pwo and 1 1/2 ours later another hundred grams of carbs. oh did i mention i did this in about 5 months while retaining pretty much all the muscle i had? i think that swolecat would disagree with that theory as well because from what i have heard from others as well as him he is an advocate of high glycemic carbs for pwo, and that goes for his cutting program as well. and if any of you know his track record hes pretty successful in reducing ones bodyfat while simultaneously retaining muscle. and i think he is highly regarded as one of the best in this area. so to each his own, but id go with something more proven.
10-19-2005, 11:45 AM #18
yes we are not saying high gi carbs doesnt work. We are just saying low gi carbs works just as good with less fat storage and more health advantages.
Glycogen replenishment takes place if you drink dextrose or not, the rate of the replenishment is of no importance. Protein synthesis is at its highest 24 hours post workout so that is when the body as the most needs the aminoacid present.
Basicly the muscles gets all it needs from low gi carbs and aminoacids, the high gi carbs has no advantage according to those studies I have seen and from reading what some highely educated people in the area has written. The topic has some controversy and all doesnt aggre with it. But I am convinced and my own experience so far(and giantz and ironfreaks)shows that the gi pwo doesnt make a difference. Thats why I said one should try both.
Hyperglycemia and hyperinsulinimia is never healthy. Not post workout, never. So if putting your body in that state has no lbm advantage why do it 4 times a week?
I have aswell lost lots of weight with high gi post workout. If you lose fat or not depends on the diet through out the day and doesnt depend that much on pwo meal.
10-19-2005, 11:47 AM #19
First off there is a 30-60min phase of rapid glycogen synthesis that is Independant of insulin . So spiking is not needed. Nutrients will be transported to the cells no matter what. Exersice increases Glut-4 permeability, as well as increases the amount of recpotors on the cell. Spikin insulin has also shown to not have any effect on protein synthesis so I ask again. Why do you say spike? Please provide proof, some thing at all. I will list what references I have made below:
Exercise-Induced Transcription of the Muscle
Glucose Transporter (GLUT 4) GenePaul S. MacLean,*,1Donghai Zheng,† Jared P. Jones,† Ann Louise Olson,‡ and G. Lynis Dohm††Department of Biochemistry, Brody
Department of Biochemistry and Molecular Biology, University of Oklahoma Health Science Center,
Oklahoma City, Oklahoma 73190; and *Center for Human Nutrition, University of Colorado
We and others have shown that exercise training increases the amount of GLUT4 mRNA and protein in skeletal muscle (4, 10 –14) and that this training induced increase in GLUT-4 increases glucose transport and improves whole body glucose tolerance.
Determinants of post-exercise glycogen synthesis during short-term recovery.
Jentjens R, Jeukendrup A.
Human Performance Laboratory, School of Sport and Exercise Sciences, University of Birmingham, Edgbaston, Birmingham, UK.
The pattern of muscle glycogen synthesis following glycogen-depleting exercise occurs in two phases. Initially, there is a period of rapid synthesis of muscle glycogen that does not require the presence of insulin and lasts about 30-60 minutes. This rapid phase of muscle glycogen synthesis is characterised by an exercise-induced translocation of glucose transporter carrier protein-4 to the cell surface, leading to an increased permeability of the muscle membrane to glucose. Following this rapid phase of glycogen synthesis, muscle glycogen synthesis occurs at a much slower rate and this phase can last for several hours. Both muscle contraction and insulin have been shown to increase the activity of glycogen synthase, the rate-limiting enzyme in glycogen synthesis. Furthermore, it has been shown that muscle glycogen concentration is a potent regulator of glycogen synthase. Low muscle glycogen concentrations following exercise are associated with an increased rate of glucose transport and an increased capacity to convert glucose into glycogen.The highest muscle glycogen synthesis rates have been reported when large amounts of carbohydrate (1.0-1.85 g/kg/h) are consumed immediately post-exercise and at 15-60 minute intervals thereafter, for up to 5 hours post-exercise. When carbohydrate ingestion is delayed by several hours, this may lead to ~50% lower rates of muscle glycogen synthesis. The addition of certain amino acids and/or proteins to a carbohydrate supplement can increase muscle glycogen synthesis rates, most probably because of an enhanced insulin response. However, when carbohydrate intake is high (>/=1.2 g/kg/h) and provided at regular intervals, a further increase in insulin concentrations by additional supplementation of protein and/or amino acids does not further increase the rate of muscle glycogen synthesis. Thus, when carbohydrate intake is insufficient (<1.2 g/kg/h), the addition of certain amino acids and/or proteins may be beneficial for muscle glycogen synthesis. Furthermore, ingestion of insulinotropic protein and/or amino acid mixtures might stimulate post-exercise net muscle protein anabolism. Suggestions have been made that carbohydrate availability is the main limiting factor for glycogen synthesis. A large part of the ingested glucose that enters the bloodstream appears to be extracted by tissues other than the exercise muscle (i.e. liver, other muscle groups or fat tissue) and may therefore limit the amount of glucose available to maximise muscle glycogen synthesis rates. Furthermore, intestinal glucose absorption may also be a rate-limiting factor for muscle glycogen synthesis when large quantities (>1 g/min) of glucose are ingested following exercise.
Carbohydrate nutrition before, during, and after exercise.
The role of dietary carbohydrates (CHO) in the resynthesis of muscle and liver glycogen after prolonged, exhaustive exercise has been clearly demonstrated. The mechanisms responsible for optimal glycogen storage are linked to the activation of glycogen synthetase by depletion of glycogen and the subsequent intake of CHO. Although diets rich in CHO may increase the muscle glycogen stores and enhance endurance exercise performance when consumed in the days before the activity, they also increase the rate of CHO oxidation and the use of muscle glycogen. When consumed in the last hour before exercise, the insulin stimulated-uptake of glucose from blood often results in hypoglycemia, greater dependence on muscle glycogen, and an earlier onset of exhaustion than when no CHO is fed. Ingesting CHO during exercise appears to be of minimal value to performance except in events lasting 2 h or longer. The form of CHO (i.e., glucose, fructose, sucrose) ingested may produce different blood glucose and insulin responses, but the rate of muscle glycogen resynthesis is about the same regardless of the structure.
Insulin sensitivity of protein and glucose metabolism in human forearm skeletal muscle.
Louard RJ, Fryburg DA, Gelfand RA, Barrett EJ.
Department of Internal Medicine, Yale University School of Medicine, New Haven, Connecticut 06510.
Physiologic increases of insulin promote net amino acid uptake and protein anabolism in forearm skeletal muscle by restraining protein degradation. The sensitivity of this process to insulin is not known. Using the forearm perfusion method, we infused insulin locally in the brachial artery at rates of 0.00 (saline control), 0.01, 0.02, 0.035, or 0.05 mU/min per kg for 150 min to increase local forearm plasma insulin concentration by 0, approximately 20, approximately 35, approximately 60, and approximately 120 microU/ml (n = 35). L-[ring-2,6-3H]phenylalanine and L-[1-14C]leucine were infused systemically, and the net forearm balance, rate of appearance (Ra) and rate of disposal (R(d)) of phenylalanine and leucine, and forearm glucose balance were measured basally and in response to insulin infusion. Compared to saline, increasing rates of insulin infusion progressively increased net forearm glucose uptake from 0.9 mumol/min per 100 ml (saline) to 1.0, 1.8, 2.4, and 4.7 mumol/min per 100 ml forearm, respectively. Net forearm balance for phenylalanine and leucine was significantly less negative than basal (P < 0.01 for each) in response to the lowest dose insulin infusion, 0.01 mU/min per kg, and all higher rates of insulin infusion. Phenylalanine and leucine R(a) declined by approximately 38 and 40% with the lowest dose insulin infusion. Higher doses of insulin produced no greater effect (decline in R(a) varied between 26 and 42% for phenylalanine and 30-50% for leucine). In contrast, R(d) for phenylalanine and leucine did not change with insulin. We conclude that even modest increases of plasma insulin can markedly suppress proteolysis, measured by phenylalanine R(a), in human forearm skeletal muscle. Further increments of insulin within the physiologic range augment glucose uptake but have little additional effect on phenylalanine R(a) or balance. These results suggest that proteolysis in human skeletal muscle is more sensitive than glucose uptake to physiologic increments in insulin.
Insulin and insulin-like growth factor-I enhance human skeletal muscle protein anabolism during hyperaminoacidemia by different mechanisms.
Fryburg DA, Jahn LA, Hill SA, Oliveras DM, Barrett EJ.
Department of Internal Medicine, University of Virginia Health Sciences Center, Charlottesville 22908, USA.
Insulin inhibits proteolysis in human muscle thereby increasing protein anabolism. In contrast, IGF-I promotes muscle protein anabolism principally by stimulating protein synthesis. As increases or decreases of plasma amino acids may affect protein turnover in muscle and also alter the muscle's response to insulin and/or IGF-I, this study was designed to examine the effects of insulin and IGF-I on human muscle protein turnover during hyperaminoacidemia. We measured phenylalanine balance and [3H]-phenylalanine kinetics in both forearms of 22 postabsorptive adults during a continuous [3H] phenylalanine infusion. Measurements were made basally and at 3 and 6 h after beginning a systemic infusion of a balanced amino acid mixture that raised arterial phenylalanine concentration about twofold. Throughout the 6 h, 10 subjects received insulin locally (0.035 mU/min per kg) into one brachial artery while 12 other subjects were given intraaterial IGF-I (100 ng/min per kg) to raise insulin or IGF-I concentrations, respectively, in the infused arm. The contralateral arm in each study served as a simultaneous control for the effects of amino acids (aa) alone. Glucose uptake and lactate release increased in the insulin- and IGF-I-infused forearms (P < 0.01) but did not change in the contralateral (aa alone) forearm in either study. In the aa alone arm in both studies, hyperaminoacidemia reversed the postabsorptive net phenylalanine release by muscle to a net uptake (P < 0.025, for each) due to a stimulation of muscle protein synthesis. In the hormone-infused arms, the addition of either insulin or IGF-I promoted greater positive shifts in phenylalanine balance than the aa alone arm (P < 0.01). With insulin, the enhanced anabolism was due to inhibition of protein degradation (P < 0.02), whereas IGF-I augmented anabolism by a further stimulation of protein synthesis above aa alone (P < 0.02). We conclude that: (a) hyperaminoacidemia specifically stimulates muscle protein synthesis; (b) insulin, even with hyperaminoacidemia, improves muscle protein balance solely by inhibiting proteolysis; and (c) hyperaminoacidemia combined with IGF-I enhances protein synthesis more than either alone.
Extreme hyperinsulinemia unmasks insulin's effect to stimulate protein synthesis in the human forearm.
Hillier TA, Fryburg DA, Jahn LA, Barrett EJ.
Division of Endocrinology and Metabolism, Department of Internal Medicine, and General Clinical Research Center, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908, USA.
Insulin clearly stimulates skeletal muscle protein synthesis in vitro. Surprisingly, this effect has been difficult to reproduce in vivo. As in vitro studies have typically used much higher insulin concentrations than in vivo studies, we examined whether these concentration differences could explain the discrepancy between in vitro and in vivo observations. In 14 healthy volunteers, we raised forearm insulin concentrations 1,000-fold above basal levels while maintaining euglycemia for 4 h. Amino acids (AA) were given to either maintain basal arterial (n = 4) or venous plasma (n = 6) AA or increment arterial plasma AA by 100% (n = 4) in the forearm. We measured forearm muscle glucose, lactate, oxygen, phenylalanine balance, and [3H]phenylalanine kinetics at baseline and at 4 h of insulin infusion. Extreme hyperinsulinemia strongly reversed postabsorptive muscle's phenylalanine balance from a net release to an uptake (P < 0.001). This marked anabolic effect resulted from a dramatic stimulation of protein synthesis (P < 0.01) and a modest decline in protein degradation. Furthermore, this effect was seen even when basal arterial or venous aminoacidemia was maintained. With marked hyperinsulinemia, protein synthesis increased further when plasma AA concentrations were also increased (P < 0.05). Forearm blood flow rose at least twofold with the combined insulin and AA infusion (P < 0.01), and this was consistent in all groups. These results demonstrate an effect of high concentrations of insulin to markedly stimulate muscle protein synthesis in vivo in adults, even when AA concentrations are not increased. This is similar to prior in vitro reports but distinct from physiological hyperinsulinemia in vivo where stimulation of protein synthesis does not occur. Therefore, the current findings suggest that the differences in insulin concentrations used in prior studies may largely explain the previously reported discrepancy between insulin action on protein synthesis in adult muscle in vivo vs. in vitro.
Observations of branched-chain amino acid administration in humans.
Department of Medicine, University of Vermont, Burlington, 05405, USA. Dwight.Matthews@uvm.edu
Since the in vitro study of Buse and Reid in 1975 showing a stimulatory effect of leucine upon rat muscle protein synthesis and reduction in proteolysis, a similar effect has been sought in humans. In 1978, Sherwin demonstrated in humans an improvement in N balance with infusion of leucine in obese subjects fasting to lose weight. A variety of subsequent studies have been performed in humans where leucine alone or the BCAAs have been administered in varying amounts and durations, and the effect upon protein metabolism has been measured. Measurements of changes in muscle amino acid metabolism were made by arteriovenous difference measurements and by biopsies. An anabolic effect of leucine and the branched-chain amino acids (BCAAs) on reduction of muscle protein breakdown was found in these studies, with no measured effect upon muscle protein synthesis. Later studies using stable isotope tracers to define both whole-body protein turnover and leg or arm protein metabolism have similarly concluded that leucine administration specifically induces a reduction in protein breakdown without increasing protein synthesis. This anabolic effect, produced through a reduction of protein breakdown in vivo in humans by leucine is contrary to in vitro studies of rat muscle where stimulation of protein synthesis, has been demonstrated by leucine. Likewise an increase in protein synthesis has also been demonstrated by insulin in rat muscle that is not seen in humans. Of the various studies administering BCAAs or leucine to humans for varying periods of time and amount, the results have been consistent. In addition, no untoward effects have been reported in any of these studies from infusion of the BCAAs at upward 3 times basal flux or 6 times normal dietary intake during the fed portion of the day.
Physiological hyperinsulinemia stimulates p70(S6k) phosphorylation in human skeletal muscle.
Hillier T, Long W, Jahn L, Wei L, Barrett EJ.
Department of Internal Medicine, Division of Endocrinology, University of Virginia School of Medicine, Charlottesville, Virginia 22908, USA.
Using tracer methods, insulin stimulates muscle protein synthesis in vitro, an effect not seen in vivo with physiological insulin concentrations in adult animals or humans. To examine the action of physiological hyperinsulinemia on protein synthesis using a tracer-independent method in vivo and identify possible explanations for this discrepancy, we measured the phosphorylation of ribosomal protein S6 kinase (P70(S6k)) and eIF4E-binding protein (eIF4E-BP1), two key proteins that regulate messenger ribonucleic acid translation and protein synthesis. Postabsorptive healthy adults received either a 2-h insulin infusion (1 mU/min.kg; euglycemic insulin clamp; n = 6) or a 2-h saline infusion (n = 5). Vastus lateralis muscle was biopsied at baseline and at the end of the infusion period. Phosphorylation of P70(S6k) and eIF4E-BP1 was quantified on Western blots after SDS-PAGE. Physiological increments in plasma insulin (42 +/- 13 to 366 +/- 36 pmol/L; P: = 0.0002) significantly increased p70(S6k) (P: < 0.01), but did not affect eIF4E-BP1 phosphorylation in muscle. Plasma insulin declined slightly during saline infusion (P: = 0.04), and there was no change in the phosphorylation of either p70(S6k) or eIF4E-BP1. These findings indicate an important role of physiological hyperinsulinemia in the regulation of p70(S6k) in human muscle. This finding is consistent with a potential role for insulin in regulating the synthesis of that subset of proteins involved in ribosomal function. The failure to enhance the phosphorylation of eIF4E-BP1 may in part explain the lack of a stimulatory effect of physiological hyperinsulinemia on bulk protein synthesis in skeletal muscle in vivo.
Ok here's what I got, now what do you have? By the way no one said Dextrose doesn't work all, we're just saying a spike is not needed and rate of glycogen replenishment has very little to do with anabolism.
10-19-2005, 12:06 PM #20
like i said , to each his own. hi gi carbs are what work best for me pwo. so based on that FACT, and it is a fact because no studies can tell me what works best for me besides my own body. everybody is different. so i need no science to back that up.i dont like relying on studies to tell me what i should and shouldnt do . you need to find what works best for you. and through my own trial and error i have found that hi gi is best for me. so that being said superfat, see what works best for you and go from there.
10-19-2005, 12:16 PM #21
well jdh just curious have you tried using low gi carbs pwo?
10-19-2005, 12:22 PM #22
How did I know you would go for the "I know what works best for me" approach. Well no shit, no one said it didn't work. I just simply refuted your claim and you cannot back up what you said. The simple fact there is a reason something works and science can explain it. So all you have offered is a testimonial and no proof. Sorry but that doesn't work for me nor should it for anyone else.
Last edited by Giantz11; 10-19-2005 at 12:33 PM.
10-19-2005, 02:40 PM #23
wow some seriously good reading there
i always assumed that dextrose or some other form of high GI carb was optimal for glycogen replenishment
(and its easy to get this impression from the things we read- i bel;ieve most other people are under similar misconceptions)
good info, i may cut back or stop completely my dex supplementation after reading that
GIANTZ where do you get all this info from - the journals and medical papers? how come i can never find stuff like that????
10-19-2005, 02:44 PM #24
g-force. Pubmed is your best friend
just noticed giantz name is green. Congrats bro
10-19-2005, 02:47 PM #25
[QUOTE=Giantz11] Although diets rich in CHO may increase the muscle glycogen stores and enhance endurance exercise performance when consumed in the days before the activity, they also increase the rate of CHO oxidation and the use of muscle glycogen. When consumed in the last hour before exercise, the insulin stimulated-uptake of glucose from blood often results in hypoglycemia, greater dependence on muscle glycogen, and an earlier onset of exhaustion than when no CHO is fed. [QUOTE=Giantz11]
just one point giantz - i remember in a thread the other day when you were replying to xtinaunasty you said that a pro/carb meal was optimal before your workout, rather than a pro/fat
what gives - do u mean a pro/carb meal, wait 2 hours and then train
10-19-2005, 02:48 PM #26Originally Posted by johan
yeah i just noticed that - how come your not a Diet guru? how do you become a guru anyway?
congratulations anyway - u deserve it
Johan what is pubmed???
Last edited by G-Force; 10-19-2005 at 02:50 PM.
10-19-2005, 02:52 PM #27
Me? Well I dont consider myself a diet guru My participation in this forum isnt that strong anymore either cause of time constrains My custom title if any should be "the vitamin nutcase"
pubmed is a medical search engine containing just about every studie done since the 50's or so(or well atleast the abstracts, the whole things usualy cost to read).
Remember thought that the abstracts doesnt always tell the whole story and the way they did the studie is just as important as the results.
10-19-2005, 02:57 PM #28
just noticed you wjere refering to giantz but quting me
when I think about hit giantz color is a bit paler then vet green. Maby the board has gotten a new guru mode??
10-19-2005, 02:59 PM #29
Hahaha mines a puke Green, Johan should be Vit C All-Star!!! Lol
10-19-2005, 03:01 PM #30
The reason I say Pro/Carb before working out is this:
Timing of amino acid-carbohydrate ingestion alters anabolic response of muscle to resistance exercise.
Tipton KD, Rasmussen BB, Miller SL, Wolf SE, Owens-Stovall SK, Petrini BE, Wolfe RR.
Department of Surgery, University of Texas Medical Branch, Galveston, Texas 77550, USA. firstname.lastname@example.org
The present study was designed to determine whether consumption of an oral essential amino acid-carbohydrate supplement (EAC) before exercise results in a greater anabolic response than supplementation after resistance exercise. Six healthy human subjects participated in two trials in random order, PRE (EAC consumed immediately before exercise), and POST (EAC consumed immediately after exercise). A primed, continuous infusion of L-[ring-(2)H(5)]phenylalanine, femoral arteriovenous catheterization, and muscle biopsies from the vastus lateralis were used to determine phenylalanine concentrations, enrichments, and net uptake across the leg. Blood and muscle phenylalanine concentrations were increased by approximately 130% after drink consumption in both trials. Amino acid delivery to the leg was increased during exercise and remained elevated for the 2 h after exercise in both trials. Delivery of amino acids (amino acid concentration times blood flow) was significantly greater in PRE than in POST during the exercise bout and in the 1st h after exercise (P < 0.05). Total net phenylalanine uptake across the leg was greater (P = 0.0002) during PRE (209 +/- 42 mg) than during POST (81 +/- 19). Phenylalanine disappearance rate, an indicator of muscle protein synthesis from blood amino acids, increased after EAC consumption in both trials. These results indicate that the response of net muscle protein synthesis to consumption of an EAC solution immediately before resistance exercise is greater than that when the solution is consumed after exercise, primarily because of an increase in muscle protein synthesis as a result of increased delivery of amino acids to the leg.
10-19-2005, 03:02 PM #31Originally Posted by johan
10-19-2005, 03:10 PM #32Originally Posted by Giantz11
right, so a pro/ carb meal before exercise will increase delivery of amino acids (or was that refering to a whey/carb shake?)
BUT it will also cause you to burn muscle glycogen quicker as u are in a mild state of hypoglycemia, so your muscles will get tired quicker
so what is a fecker meant to do?
10-19-2005, 03:18 PM #33
Well weight lifting is a little more taxing to the ATP/CN system anways. So glycogen depletion is very overrated. But if you do perhaps burn more, that does nothing more than unsure greater nutrient partitioning since even more carbs will be directed towards the muscles. Not a bad thing. It makes sense to have aminos before to maximize delivery when blood flow to the area is at its peak.
10-19-2005, 03:29 PM #34Originally Posted by Giantz11
yep i can go along with that cheers
10-19-2005, 03:30 PM #35
great info. And, love that you back up what you say with actual science and published science at that. Come next spring I will be published! Not in a fitness or related subject however.
10-19-2005, 03:34 PM #36
Congrats buddy! What topic might I ask?
10-19-2005, 03:44 PM #37Originally Posted by Giantz11
I work with pathogenic Neisseria (the std variety if you are familiar, if not no biggie). I will be first author on a paper dealing with reinfection in mice. I am going to a big conference in May call ASM (American Society of Microbiology) where I will let people know about my research. I am really happy to just be a first author in a published journal!
10-19-2005, 03:46 PM #38Originally Posted by Lunacy
10-19-2005, 03:51 PM #39Originally Posted by Giantz11
10-19-2005, 04:06 PM #40Originally Posted by Lunacy
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