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    Quote Originally Posted by ozzman' post='459157' date='Feb 18 2008, 06:02 PM
    unfortunately, then I would have to add some lactaid


    Maybe not...the carbs they get rid of must mostly be in the form of lactose so you may find that Calorie Countdown milk doesn't bother you too much.

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    I don't see the Hood Calorie Countdown milk much any more.

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    I'll have to give it a try, as it is cheaper than lactose free milk...Mixing it with WP that has Aminogen helps

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    Well-chewed meat is a fast acting protein.



    This may explain how I can eat two lbs of it and be hungry 3 hours later!



    From bodyrecomposition.com:



    Postprandial whole-body protein metabolism after a meat meal is influenced by chewing efficiency in elderly subjects1,2,3



    Didier Rémond, Marie Machebeuf, Claude Yven, Caroline Buffière, Laurence Mioche, Laurent Mosoni and Philippe Patureau Mirand

    1 From the Institut National de la Recherche Agronomique, UMR 1019, Unité de Nutrition Humaine, Centre de Clermont-Ferrand-Theix, Saint Genès-Champanelle, France





    Background: The rate of protein digestion affects protein utilization in elderly subjects. Although meat is a widely consumed protein source, little is known of its digestion rate and how it can be affected by the chewing capacity of elderly subjects.



    Objectives: We used a [1-13C]leucine balance with a single-meal protocol to assess the absorption rate of meat protein and to estimate the utilization of meat protein in elderly subjects with different chewing efficiency.



    Design: Twenty elderly volunteers aged 60–75 y were involved in the study. Ten of them had healthy natural dentition, and the other 10 were edentulous and wore complete dentures. Whole-body fluxes of leucine, before and after the meal (120 g beef meat), were measured with the use of a [1-13C]leucine intravenous infusion.



    Results: A rapid increase in plasma aminoacidemia and plasma leucine entry rate was observed after meat intake in dentate subjects. In complete denture wearers the increase in leucine entry rate was delayed (P < 0.05), and the amount of leucine appearing in peripheral blood during the whole postprandial period was lower than in dentate subjects (P < 0.01). Postprandial whole-body protein synthesis was lower in denture wearers than in dentate subjects (30% compared with 48% of leucine intake, respectively; P < 0.05).



    Conclusion: Meat proteins could be classified as fast digested proteins. However, this property depends on the chewing capacity of elderly subjects. This study showed that meat protein utilization for protein synthesis can be impaired by a decrease in the chewing efficiency of elderly subjects.

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    Maybe you should try some Bass

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    Quote Originally Posted by Jakeshorts' post='459281' date='Feb 19 2008, 07:16 AM
    Maybe you should try some Bass






    You were close, turns out cod is the answer



    Whereas whey, milk, and to some extent cheese ingestion

    resulted in obvious amino acid responses, the remaining meals

    (GH, GL, cod, and WWB) resulted in only small increases in

    plasma amino acids. Generally, the amino acid responses to the

    cod meal occurred 60 min after ingestion
    . In contrast, peak amino

    acid responses to milk, whey, and cheese occurred more rapidly—

    within 30–45 min after ingestion—which indicated that

    milk proteins are highly digestible and result in a rapid release of

    amino acids into the circulation



    Although whey and cod proteins are similar with respect to the

    content and distribution of amino acids, the postprandial plasma

    pattern of amino acids differed substantially after the test meals

    containing these proteins, most probably because of the different

    digestion and absorption rates of these proteins
    . It is especially

    interesting that several of the known insulinotropic amino acids

    (leucine, valine, isoleucine, lysine,andthreonine)wereamongthose

    amino acids that were observed to increase after the whey meal.



    The free full-text is online



    Glycemia and insulinemia in healthy subjects after lactoseequivalent

    meals of milk and other food proteins: the role of plasma

    amino acids and incretins1–3

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    So, here's another one...



    Either



    This 10 g/hr amino acid absorption rate can be affected by things like androgens or the PWO "window of opportunity"





    Or



    All the gearheads that preach about the body's increased "capacity to use protein" while on cycle are retarded, and they are misunderstanding

    the rate-limiting step here.

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    Probably the latter, but you forgot to post the research!



    EDIT: Just saw your edit

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    BUMP on androgens/PWO window and increased AA absorption kinetics? Otherwise why would whey hydrosylate be superior to slower PRO in the PWO window in trained individual (yall know the study)...



    AND --



    Consider the combination of this thread and the low-carb threads we have going currently.



    Fat slows gastric emptying... so using a whey shake as an example (~24 g fast PRO), can we find the approximate amount of fat that could approximate the "2.3 g every 20 minutes" absorption rate that the RPT-WP method found superior? Whey + DAG at that ratio could be killer -- not sure if this ratio should be altered pre or PWO though.



    As an aside, does anyone else wonder if these absorption kinetics match fairly well to the gastric release rate of a meat+fat meal (perhaps a common meal for evolutionary ancestors?)

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    If only ~10g of protein and ~15g of fat can be absorbed per hour, does that not set a daily limit of about 240g and 360g, respectively?



    If it does then that's a maximum of 4300 cals per day that could be absorbed from those macronutrients, right?

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    Quote Originally Posted by rock_ten' post='461708' date='Feb 27 2008, 03:58 PM
    If only ~10g of protein and ~15g of fat can be absorbed per hour, does that not set a daily limit of about 240g and 360g, respectively?



    If it does then that's a maximum of 4300 cals per day that could be absorbed from those macronutrients, right?


    In theory, yes. YMMV.

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    Senior Member Marc McDougal's Avatar
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    I eat 420g a day.



    Do I win?




    Body of Evidence Blog



    "If you're going to be crazy, you have to get paid for it or else you're going to be locked up." -HST

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    Quote Originally Posted by Marc McDougal' post='461745' date='Feb 27 2008, 05:45 PM
    I eat 420g a day.



    Do I win?


    If its 420g of CHO, you sure do!

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    Senior Member Jay Black's Avatar
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    Quote Originally Posted by dashforce' post='461663' date='Feb 27 2008, 02:02 PM
    BUMP on androgens/PWO window and increased AA absorption kinetics? Otherwise why would whey hydrosylate be superior to slower PRO in the PWO window in trained individual (yall know the study)...



    AND --



    Consider the combination of this thread and the low-carb threads we have going currently.



    Fat slows gastric emptying... so using a whey shake as an example (~24 g fast PRO), can we find the approximate amount of fat that could approximate the "2.3 g every 20 minutes" absorption rate that the RPT-WP method found superior? Whey + DAG at that ratio could be killer -- not sure if this ratio should be altered pre or PWO though.



    As an aside, does anyone else wonder if these absorption kinetics match fairly well to the gastric release rate of a meat+fat meal (perhaps a common meal for evolutionary ancestors?)
    Bump.
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  15. #35
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    BUMP on androgens/PWO window and increased AA absorption kinetics? Otherwise why would whey hydrosylate be superior to slower PRO in the PWO window in trained individual (yall know the study)...



    -----------------------------------



    I had posted this one in the IF thread:



    Am J Physiol Regul Integr Comp Physiol. 2007 Nov 21; [Epub ahead of print]

    Resistance training alters the response of fed-state mixed muscle protein synthesis in young men.

    Tang JE, Perco JG, Moore DR, Wilkinson SB, Phillips SM.

    Kinesiology, McMaster University, Hamilton, Canada.



    Ten healthy young men (21.0 +/- 1.5 yr, 1.79 +/- 0.1 m, 82.7 +/- 14.7 kg, mean +/- SD) participated in eight weeks of intense unilateral resistance training (knee extension exercise) such that one leg was trained (T) and the other acted as an untrained (UT) control. After the eight weeks of training, infusions of L-[ring-d5] phenylalanine, L-[ring-(13)C6] phenylalanine, and d3 alpha-KIC were used to measure mixed muscle protein synthesis in the T and UT legs by the direct incorporation method (FSR). Protein synthesis was determined at rest, 4 and 28 h after an acute bout of resistance exercise performed at the same intensity relative to the gain in strength before and after training. Training increased mean muscle fibre cross-sectional area only in the T leg (type I: 16 +/- 10 %; type II: 20 +/- 19 %, P < 0.05). Muscle protein FSR in both legs at 4 h (T: 162 +/- 76 %; UT: 108 +/- 62 %, P < 0.01 versus rest) with the increase in the T leg being significantly higher than in the UT leg at this time (P < 0.01). At 28 h post-exercise, FSR in the T leg had returned to resting levels; however, the rate of protein synthesis in the UT leg remained elevated above resting (70 +/- 49%, P < 0.01). We conclude that resistance training attenuates the protein synthetic response to acute resistance exercise, despite higher initial increases in FSR, by shortening the duration for which protein synthesis is elevated. Key words: hypertrophy, feeding, weightlifting.



    It would be nice to know what happens btw 4 and 28 hours. i.e. at what time does protein synthesis actually stops in the trained muslce?



    This one is yours from the "post-exercise carbs a waste" thread:



    Short-term insulin and nutritional energy provision do not stimulate muscle protein synthesis if blood amino acid availability decreases.

    Bell JA, Fujita S, Volpi E, Cadenas JG, Rasmussen BB.



    Sealy Center on Aging & Stark Diabetes Center, Department of Physical Therapy, University of Texas Medical Branch, 301 University Blvd., Galveston, TX 77555-1144, USA.



    Muscle protein synthesis requires energy and amino acids to proceed and can be stimulated by insulin under certain circumstances. We hypothesized that short-term provision of insulin and nutritional energy would stimulate muscle protein synthesis in healthy subjects only if amino acid availability did not decrease. Using stable isotope techniques, we compared the effects on muscle phenylalanine kinetics across the leg of an amino acid-lowering, high-energy (HE, n = 6, 162 +/- 20 kcal/h) hyperglycemic hyperlipidemic hyperinsulinemic clamp with systemic insulin infusion to a low-energy (LE, n = 6, 35 +/- 3 kcal/h, P < 0.05 vs. HE) euglycemic hyperinsulinemic clamp with local insulin infusion in the femoral artery. Basal blood phenylalanine concentrations and phenylalanine net balance, muscle protein breakdown, and synthesis (nmol.min(-1).100 g leg muscle(-1)) were not different between groups. During insulin infusion, femoral insulinemia increased to a similar extent between groups and blood phenylalanine concentration decreased 27 +/- 3% in the HE group but only 9 +/- 2% in the LE group (P < 0.01 HE vs. LE). Phenylalanine net balance increased in both groups, but the change was greater (P < 0.05) in the LE group. Muscle protein breakdown decreased in the HE group (58 +/- 12 to 35 +/- 7 nmol.min(-1).100 g leg muscle(-1)) and did not change in the LE group. Muscle protein synthesis was unchanged in the HE group (39 +/- 6 to 30 +/- 7 nmol.min(-1).100 g leg muscle(-1)) and increased (P < 0.05) in the LE group (41 +/- 9 to 114 +/- 26 nmol.min(-1).100 g leg muscle(-1)). We conclude that amino acid availability is an important factor in the regulation of muscle protein synthesis in response to insulin, as decreased blood amino acid concentrations override the positive effect of insulin on muscle protein synthesis even if excess energy is provided.



    Taken together, a need for very rapid AA availability is suggested. [Given a 4-hour window, seems whey would be fast enough though.]



    Contrast this, however, with the study showing whole milk to be more effective than skim PWO: http://www.mindandmuscle.net/forum/index.p...st&p=449315 .



    And then this one ( http://www.mindandmuscle.net/forum/index.p...st&p=449402 ) suggesting that total milk protein is better than casein is better than whey (i.e. the slower the better).



    Note the two milk studies were conducted with 'volunteers,' rather than trained individuals. That may make all the difference.



    -----------------------------------



    As an aside, does anyone else wonder if these absorption kinetics match fairly well to the gastric release rate of a meat+fat meal (perhaps a common meal for evolutionary ancestors?)



    I posted a study in the first page of this thread suggesting that well-chewed meat is a fast-acting protein.

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    Well, we know about PRO synthesis being upregulated, we know that the AA pool size is critical and can be rate limiting, but my question still remains:



    Is amino acid absorption (from the gut) altered PWO or with androgen use? Or does the 10g/hr stated in the OP still hold true?



    And post workout, in trained individuals, I thought the faster the better (indicating altered absorption perhaps? -- I can't find the study ATM, I have it at home though so I'll post it later).



    EDIT: And that study just says "fast protein" without including any numbers -- do you have the FT? Can we get numbers so as to compare with whey/casein/isolates/hydrolysates?

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    Quote Originally Posted by dashforce' post='462041' date='Feb 28 2008, 10:29 AM
    And post workout, in trained individuals, I thought the faster the better



    Is there some reason to believe this study is the definitive one? Swear I've read casein + whey > casein > whey, but can't recall if subjects were trained or not. I can check the protein book this evening.



    I thought the faster the better (indicating altered absorption perhaps?)



    No, I think it's due to the shorter window of opportunity described in the study I posted above. Protein synthesis in the trained muscle shuts down after four hours.





    EDIT: And that study just says "fast protein" without including any numbers -- do you have the FT? Can we get numbers so as to compare with whey/casein/isolates/hydrolysates?



    Plasma aminos peak 1 -2 hrs after beef meal in young subjects. You have mail.

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    Is there some reason to believe this study is the definitive one? Swear I've read casein + whey > casein > whey, but can't recall if subjects were trained or not. I can check the protein book this evening.



    Well, no -- but it was done in well trained athletes post-workout, exactly our situation. I found the study, but you can't attach files in this forum... I'll cite it later, in a big hurry ATM



    No, I think it's due to the shorter window of opportunity described in the study I posted above. Protein synthesis in the trained muscle shuts down after four hours.



    Damn -- good point. (interior *click* as the idea falls into place)



    EDIT: Thinking about it, this still suggests that the intestinal AA absorption is accelerated in the PWO window, right?








    Plasma aminos peak 1 -2 hrs after beef meal in young subjects. You have mail.



    Thanks. As do you.


  19. #39
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    Abstract from study Dash sent is below.



    The subjects added 0.68 g/lb of hydro-whey or casein, but only increased their total intake from about 0.8 g/lb to .95 g/lb. So whole food protein were replaced with supplements, and intakes remained low by body building standards. The hydro-whey group had better lean mass and strength gains, and dropped body fat.



    From trueprotein.com: casein has 0.016 g Cystine/gram, hydro-whey high grade has 0.056g/g, and hydro-whey ultra grade has 0.1g/g. Whey is also higher in essential aminos than casein.



    With ~70% of the protein intake coming from a supplement during the study, the above cannot be overlooked.



    All we can really conclude is that replacing a large portion of whole food protein with hydro-whey is better than replacement with casein.



    Would additional whole food protein have had the same effect?



    --------------------------------------------------------------



    THE EFFECT OF WHEY ISOLATE AND RESISTANCE TRAINING ON STRENGTH, BODY COMPOSITION AND PLASMA GLUTAMINE



    It is well established that athletes undertaking intense resistance training programs require higher dietary protein intakes. However very few studies have addressed what type of protein is optimal to enhance stength gains from weight training exercise.



    PURPOSE:

    This study examined the effects of two commonly used dietary protein supplements, whey isolate and casein, on strength, body composition and plasma glutamine levels during a 10-week intense resistance training program.



    METHODS:

    In a randomized, double-blind protocol thirteen resistance-trained males (age: 25.5 ± 2.7, 26.1 ± 2.1 yrs; weight: 84.0 ± 2.0, 79.7 ± 4.2 mean ± SEM for whey (n = 6) and casein (n = 7) groups, respectively) supplemented their normal diet with either a 100% whey isolate or casein (1.5gms/kg body wt/day) for 10 weeks. All subjects undertook the same fully supervised resistance training program three days per week. Written three-day food recordings were completed by the bodybuilders to demonstrate that subject's normal eating patterns were maintained throughout the study. Strength was assessed by 1-RM in the barbell bench press, squat and pull down. Body composition was assessed by DEXA (QDR4500). Plasma glutamine levels were determined by an enzymatic method with spectroscopic detection. All assessments occurred in the week prior, to and the week following training.



    RESULTS:

    The whey isolate group achieved a significantly greater gain (P < 0.01) in lean mass (4.99 ± 0.25) than the casein group (0.81 ± 0.43kg). While both groups significantly increased (P < 0.05) strength in the three exercises assessed, the whey isolate group made greater strength increases (P < 0.05) in all three exercises compared to the casein group. The whey isolate group also showed a significant decrease (P < 0.05) in fat mass (-1.46 ± 0.52kg), whereas the casein group exhibited a slight rise (0.19 ± 0.27kg). Plasma glutamine levels, pre and post training, did not change in either group.



    CONCLUSION:

    The major finding of this study was that a 100% whey isolate protein supplement was more effective at increasing muscle mass and strength and decreasing fat mass than a casein protein supplement in resistance trained athletes. Both types of protein appear to prevent a decline in plasma glutamine levels that have previously been reported with intense exercise training. Supported by AST Sports Science.

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    Quote Originally Posted by Heavy_Lifter85' post='459472' date='Feb 19 2008, 06:39 PM




    You were close, turns out cod is the answer



    Whereas whey, milk, and to some extent cheese ingestion

    resulted in obvious amino acid responses, the remaining meals

    (GH, GL, cod, and WWB) resulted in only small increases in

    plasma amino acids. Generally, the amino acid responses to the

    cod meal occurred 60 min after ingestion
    . In contrast, peak amino

    acid responses to milk, whey, and cheese occurred more rapidly—

    within 30–45 min after ingestion—which indicated that

    milk proteins are highly digestible and result in a rapid release of

    amino acids into the circulation



    Although whey and cod proteins are similar with respect to the

    content and distribution of amino acids, the postprandial plasma

    pattern of amino acids differed substantially after the test meals

    containing these proteins, most probably because of the different

    digestion and absorption rates of these proteins
    . It is especially

    interesting that several of the known insulinotropic amino acids

    (leucine, valine, isoleucine, lysine,andthreonine)wereamongthose

    amino acids that were observed to increase after the whey meal.



    The free full-text is online



    Glycemia and insulinemia in healthy subjects after lactoseequivalent

    meals of milk and other food proteins: the role of plasma

    amino acids and incretins1–3
    fiber.
    Man on a mission

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