I'm 5'7 and about 160 pounds....I'm not skinny by any means, nor am I overly obese. Problem is, I have some excess fat here and there that I haven't burned off from my teens. I work out regularly...about 3 times a week but I'm not trying to gain much weight, just kind of tone/lean out. I was just curious as to whether or not it would be necessary/a benefit for me to take protein after my workouts? I'm a bit new to the workout thing so any help would be appreciated. Thanks a bunch.
rockwolf2001
12-18-2009, 10:17 PM
Originally posted by wintonyk
You don't need to eat crazy amounts of protein per day, but 30g post workout will get you body going on recovery. Anything more then that unfortunately can't be processed in a single sitting.
quick question, does every human max out at 30g, or if you're a bigger/smaller person do you max out at a larger/smaller amount?
Despair*
12-18-2009, 10:57 PM
Originally posted by wintonyk
You don't need to eat crazy amounts of protein per day, but 30g post workout will get you body going on recovery. Anything more then that unfortunately can't be processed in a single sitting. I have a reference for that somewhere if anyone likes I just can't seem to find it right now.
Don't mean to refute your info wintonyk, but I thought the max dosage you can process was around 50-60g in one sitting? Is this wrong? I've seen a lot of guys on some of their diet posts taking 50g or so of protein post workout, so I'm just wondering.
Redlined_8000
12-18-2009, 11:22 PM
Originally posted by rockwolf2001
quick question, does every human max out at 30g, or if you're a bigger/smaller person do you max out at a larger/smaller amount?
Biggest myth ever. You dont max out at 30g, that is ridiculous. Take a 80g Casein Protein shake for example, and drink it in one sitting. I guess that 50g would just be wasted right? Too bad that it will take 3-6 hours to digest all of it, a little bit at a time. Thats why its a stupid myth, even Whey Isolate takes around 90 min to spike in the bloodstream, it dosnt just get absorbed right when you drink it all at once.... Wintonyk I would really like to see a credible reference for that.
wintonyk
12-19-2009, 02:35 AM
Originally posted by suen17
Protein's main role in our body is for protein synthesis, not DNA synthesis. Ingested protein gets broken down to amino acids which in turn is used by cells to build other protein molecules.
Maybe you ought to read up on your biology.
The building blocks of life are DNA. DNA an amine group. We can agree that protein is made up of CHON. It is the only nitrogen containing compound that we absorb. So logically speaking, you need DNA to create muscle and to create DNA you need amino acids. And amino acids come from you guessed it protein.
According to Nutrition for Fitness and Sport (Melvin H. Williams, 2006) The 9 major roles of protein are as follows
1. Structural Function - Form vital constiuents of all cells in the body
2. Transport Function - Transport of various substances in the blood, such as lipoproteins
3. Enzyme Function - Form almost all enzymes in the body to regulate numerous physiological processes
4. Hormone and Neuro Transmitter function - everything from insulin to serotonin
5. Immune Function - form key components of immune system ie. antibodies
6. Acid Base Balance - Buffer to maintain optimal pH
7 Fluid Balance - Exert osmotic pressure to maintain optimal fluid balance
8. Energy Function - Provide source of energy for Kreb/TCA cycle. Excess gets converted to glucose or fat for future energy
9. Movement - using proteins to structurally contract muscles
Moderate Amounts of Protein Per Meal (http://www.sciencedaily.com/releases/2009/10/091026125543.htm)
There is the link to the news article.
And here is the reference:
Symons et al. A Moderate Serving of High-Quality Protein Maximally Stimulates Skeletal Muscle Protein Synthesis in Young and Elderly Subjects. Journal of the American Dietetic Association, 2009; 109 (9): 1582 DOI: 10.1016/j.jada.2009.06.369
Originally posted by wintonyk
The building blocks of life are DNA. DNA an amine group. We can agree that protein is made up of CHON. It is the only nitrogen containing compound that we absorb. So logically speaking, you need DNA to create muscle and to create DNA you need amino acids. And amino acids come from you guessed it protein.
Back to the books. DNA (nucleic acid) is a blueprint for protein synthesis, not a building material (amino acid).
Originally posted by wintonyk
Moderate Amounts of Protein Per Meal (http://www.sciencedaily.com/releases/2009/10/091026125543.htm)
There is the link to the news article.
And here is the reference:
Symons et al. A Moderate Serving of High-Quality Protein Maximally Stimulates Skeletal Muscle Protein Synthesis in Young and Elderly Subjects. Journal of the American Dietetic Association, 2009; 109 (9): 1582 DOI: 10.1016/j.jada.2009.06.369
1. What defines "young" and "elderly" in the study?
2. The total sample size was 34 (17+17). Come on now, can that possibly be a reasonable representation of the population?
3. Only one source of protein was tested, beef.
4. What made up the remainder of the meals?
5. There was no mention of exercise at all. You should know that our bodies don't operate the same under all conditions.
You need to do more research into the research you use for reference.
suen17
12-19-2009, 10:47 AM
Originally posted by wintonyk
The building blocks of life are DNA. DNA an amine group. We can agree that protein is made up of CHON. It is the only nitrogen containing compound that we absorb. So logically speaking, you need DNA to create muscle and to create DNA you need amino acids. And amino acids come from you guessed it protein.
Haha do you really want to go there?
Protein's main role is protein synthesis. DNA synthesis is secondary to a cell's requirements for its building blocks.
Nucleotides, while they do consist of CHON, as you put it, does indeed get elements from amino acids, but it also takes molecules from CO2, UMP, UDP, ATP, H20, formate, glutamate, glutamine, and a whackload of other enzymes and substrates. Moreover, nucleotides are NOT needed in diet as they can be made from simply aspartate and formate. Both of these amino acid analogues can be synthesized or are byproducts that DO NOT REQUIRE proteins to begin with. (Forgive me, I have not remembered much from biochemistry).
READ: in reality you do not need amino acids to build DNA/RNA.
Nonetheless, the majority of the protein that you ingest is used to build ENZYMES for metabolism and anabolism. That is where they are most used.
In the end it helps to have an excess of amino acids regardless. While some people can only USE 30g of protein at any sitting, it will always help to have excess, especially if you are working out or if you are bigger. Otherwise, you will be breaking down other cellular products in order to provide amino acids as necessary. Think equilibriums.
Redlined_8000
12-19-2009, 11:19 AM
Originally posted by wintonyk
Moderate Amounts of Protein Per Meal (http://www.sciencedaily.com/releases/2009/10/091026125543.htm)
There is the link to the news article.
And here is the reference:
Symons et al. A Moderate Serving of High-Quality Protein Maximally Stimulates Skeletal Muscle Protein Synthesis in Young and Elderly Subjects. Journal of the American Dietetic Association, 2009; 109 (9): 1582 DOI: 10.1016/j.jada.2009.06.369
That article is not all it seems. so you eat 4 oz of beef, and 12 oz of beef, yet get the same amount of protein synthesis. That is because they both get absorbed at the same rate. I would bet if they did protein synthesis tests every hour after the meal, it would soon be clear that the 12 oz will keep protein synthesis elevated for much longer.
wintonyk
12-19-2009, 04:39 PM
Originally posted by lint
Back to the books. DNA (nucleic acid) is a blueprint for protein synthesis, not a building material (amino acid).
1. What defines "young" and "elderly" in the study?
2. The total sample size was 34 (17+17). Come on now, can that possibly be a reasonable representation of the population?
3. Only one source of protein was tested, beef.
4. What made up the remainder of the meals?
5. There was no mention of exercise at all. You should know that our bodies don't operate the same under all conditions.
You need to do more research into the research you use for reference.
By definition of the human genome project DNA is "the building block for all life material.
You need to read more then just the news article. Perhaps the abstract or even the actual article. This will help answer some questions.
With this study like all studies there are limitations. It provides insight and a direction to look for in the future for larger studies. The remainder of the meals is irrelevant when talking about strictly protein consumption. Ie. it was consumed by itself.
Research
A Moderate Serving of High-Quality Protein Maximally Stimulates Skeletal Muscle Protein Synthesis in Young and Elderly Subjects
T. Brock Symons PhD, Melinda Sheffield-Moore PhD, Robert R. Wolfe PhD and Douglas Paddon-Jones PhD,
Accepted 30 January 2009. Available online 21 August 2009.
Abstract
Ingestion of sufficient dietary protein is a fundamental prerequisite for muscle protein synthesis and maintenance of muscle mass and function. Elderly people are often at increased risk for protein-energy malnutrition, sarcopenia, and a diminished quality of life. This study sought to compare changes in muscle protein synthesis and anabolic efficiency in response to a single moderate serving (113 g; 220 kcal; 30 g protein) or large serving (340 g; 660 kcal; 90 g protein) of 90% lean beef. Venous blood and vastus lateralis muscle biopsy samples were obtained during a primed, constant infusion (0.08 μmol/kg/min) of L-[ring-13C6] phenylalanine in healthy young (n=17; 34±3 years) and elderly (n=17; 68±2 years) individuals. Mixed muscle fractional synthesis rate was calculated during a 3-hour postabsorptive period and for 5 hours after meal ingestion. Data were analyzed using a two-way repeated measures analysis of variance with Tukey's pairwise comparisons. A 113-g serving of lean beef increased muscle protein synthesis by approximately 50% in both young and older volunteers. Despite a threefold increase in protein and energy content, there was no further increase in protein synthesis after ingestion of 340 g lean beef in either age group. Ingestion of more than 30 g protein in a single meal does not further enhance the stimulation of muscle protein synthesis in young and elderly.
Article Outline
Methods
Subjects and Experimental Design
Analytical Methods
Calculations
Statistical Analysis
Results and Discussion
Acknowledgements
References
Vitae
Ingestion of sufficient dietary protein is a fundamental prerequisite for muscle protein synthesis and maintenance of lean muscle mass and function. Elderly are at increased risk of protein-energy malnutrition ([1], [2] and [3]) and sarcopenic muscle loss ([4] and [5]). Although it is clear that strategies to prevent and treat sarcopenia cannot exclusively target a single issue, recent commentary and research has suggested that moderately increasing dietary protein intake above the recommended dietary allowance of 0.8 g protein/kg/day may enhance muscle protein anabolism and offer additional benefits associated with increased satiety, thermogenesis, and energy expenditure ([6], [7], [8], [9] and [10]).
We recently demonstrated that a single moderate-size serving of a protein-rich food (113 g lean beef) acutely increased muscle protein synthesis above fasting (baseline) values by 50% in both young and elderly individuals (11). A 113-g serving of 90% lean beef (220 kcal) contains approximately 30 g of protein, 10 g of essential amino acids (EAAs) and represents 50% of the Recommended Dietary Allowance for a 75-kg individual. Although the results of this earlier study were particularly encouraging for older individuals, several questions remained unanswered. Cuthbertson and colleagues (12) noted that ingestion of 2.5 g, 5 g, or 10 g of rapidly digested free-form EAAs increased myofibrillar protein synthesis in a dose-dependent manner. However, a larger 20- to 40-g serving of EAAs failed to elicit an additional stimulatory effect. In a practical sense, these data are consistent with the contention that a protein source containing approximately 10 g of EAAs provides a maximal acute protein synthetic effect. However, in the context of a more realistic meal-like setting, we do not know if a similar dose–response relationship exists in response to ingestion of a more slowly digested, high-quality intact protein such as lean beef ([13] and [14]).
Compared to a moderately sized protein meal (113 g lean beef, 30 g protein, 10 g EAAs, 220 kcal), this study sought to determine whether a threefold larger protein- and energy-rich meal (340 g lean beef, 90 g protein, 30 g EAAs, 660 kcal), representative of the exaggerated portion size available in many restaurants, can be justified by an increased ability to acutely increase muscle protein synthesis in healthy young and elderly individuals.
Methods
Subjects and Experimental Design
Participants were recruited through the Sealy Center on Aging Volunteer Registry at The University of Texas Medical Branch and through newspaper advertisements and flyers. This study was approved by the Institutional Review Board at The University of Texas Medical Branch. An independent, internal monitoring board oversaw study procedures, data collection, and analysis.
Medical screening included a medical history and physical, blood count, plasma electrolytes, blood glucose concentration, and liver and renal function tests. Eligible participants did not have any recent injury, metabolically unstable medical condition, low hematocrit or hemoglobin, vascular disease, hypertension, or cardiac abnormality. All participants were physically active and independent but not athletically trained.
Subjects were 17 young (8 male, 9 female, age 35±3 years, height 1.71±0.03 m, weight 79.2±7 kg [mean±standard deviation]) and 17 elderly (10 male, 7 female, age 68±2 years, height 1.70±0.04 m, weight 77.5±8 kg [mean±standard deviation]) individuals. Besides age, there were no between-group differences in demographic variables. Volunteers were randomly assigned to participate in one of four separate groups: young, 113-g beef group (5 male, female); young, 340-g beef group (3 male, 4 female); elderly, 113-g beef group (5 male, 5 female); and elderly, 340-g beef group (5 male, 2 female). There was no evidence of a sex effect ([15] and [16]).
For 72 hours before admission, participants were asked to maintain their normal diet and avoid strenuous activity. Participants stayed overnight in the General Clinical Research Center and were studied the following morning after an overnight fast. Subjects remained largely physically inactive (ie, rested in bed) for the duration of the study. On the morning of the study at approximately 5:30 am, an 18-gauge polyethylene catheter (Insyte-W; Becton Dickinson, Sandy, UT) was inserted into a forearm vein for blood sampling. A second 18-gauge polyethylene catheter was inserted into a forearm vein of the contralateral limb for stable isotope tracer infusion. Background blood samples were drawn for the analysis of phenylalanine enrichments and concentrations, insulin (serum separator tubes; BD Vacutainer SST, Franklin Lakes, NJ), and glucose concentrations (CapiJect tubes; Terumo Medical Corp, Elkton, MD). A primed (2 μmol/kg), constant infusion (0.08 μmol·kg−1min−1) of L- [ring-13C6] phenylalanine (Cambridge Isotope Laboratories, Andover, MA) was started and maintained for 11 hours.
During the postabsorptive period (9:00 am to 12 noon), venous blood samples were obtained hourly. Following ingestion of the lean beef meal (113 g or 340 g), venous blood samples were obtained every 20 minutes for the duration of the study (5 hours) (see Figure 1). Muscle biopsy samples, approximately 100 mg, were taken at three time points under local anesthesia (2% lidocane) from the lateral portion of the vastus lateralis of the leg using a 5-mm Bergstrom biopsy needle as previously described (17). The biopsy site was approximately 10 cm to 15 cm above the knee.
Full-size image (19K)
Figure 1. Data were collected in cohorts of young (n=17; 34±3 years) and older adults (n=17; 68±2 years) during an 11-hour stable isotope infusion protocol. Muscle biopsy and venous blood samples were obtained to calculate mixed muscle protein synthesis before and after ingestion of 113 or 340 g of lean beef.
The 90% lean ground beef patties (113 g; 220 kcal; 30 g protein, 11 g fat per patty) were prepared and supplied by Texas Tech University. Patties were precooked, individually vacuum-sealed, and frozen before delivery to The University of Texas Medical Branch. The patties were gently warmed in a microwave oven and provided to the participant without condiments immediately following the second biopsy. Participants in the higher protein group consumed three beef patties. All volunteers were able to consume the meal within 10 to 15 minutes.
Analytical Methods
All analytical methods have been described in detail previously ([11], [18] and [19]). Briefly, plasma phenylalanine was extracted by cation exchange chromatography (Dowex AG 50W-8X, 100-220 mesh H+ form; Bio-Rad Laboratories, Richmond, CA) and dried under vacuum (Savant Instruments, Farmingdale, NY). Phenylalanine enrichments and concentrations were determined with tert-butyldimethylsilyl derivative using gas chromatography-mass spectrometry (6890 Plus GC; Agilent Technologies, Palo Alto, CA) with electron impact ionization. Ions 234, 238, 240, 336, 342, and 346 were monitored ([20] and [21]).
Mixed muscle intracellular phenylalanine enrichments and concentrations were calculated with a tert-butyldimethylsilyl derivative. Mixed muscle protein-bound L- [ring-13C6] phenylalanine enrichments were determined using gas chromatography-mass spectrometry via the standard curve approach as previously described (19).
Calculations
Mixed muscle protein fractional synthesis rate (FSR) was calculated by measuring the direct incorporation of L-[ring-13C6] phenylalanine into protein, via the precursor-product model:
FSR=[(Ep2−Ep1)/(Em×t×CF)]×60×100
where Ep1 and Ep2 are the enrichments of bound L-[ring-13C6] phenylalanine in two sequential biopsies, t is the time interval between two biopsies, and Em is the mean L-[ring-13C6] phenylalanine enrichment in the muscle intracellular pool.
To account for the decreased plasma L-[ring-13C6] phenylalanine enrichment and isotopic non–steady state during the postmeal period, a correction factor (CF) was used (11).
CF=Ev(AUC)/Ev(m2,m3)
where Ev(AUC) is the actual venous enrichment area under the curve between sequential biopsies (ie, biopsy 2 and 3) (Figure 1) and Ev(m2,m3) is the average venous enrichment at each biopsy time point. This correction is based on the assumption that the transient postmeal decrease in plasma phenylalanine enrichment reflects the decrease in the muscle intracellular phenylalanine enrichment.
Statistical Analysis
Changes in muscle protein synthesis were analyzed using a two-way repeated measures analysis of variance with within (time) and between (age) group factors. Secondary analyses were done using pairwise multiple comparison procedures with Tukey correction. Data are presented as means±standard error of the mean. Statistical analysis was done using SigmaStat for Windows (version 3.5, 2007, Systat Software, Inc, San Jose, CA). Statistical significance for all analyses was accepted at α=.05.
Results and Discussion
Fasting plasma phenylalanine enrichments (tracer/tracee ratio) were similar in the moderate-protein group (young, 0.112±0.003; elderly, 0.113±0.002) and high-protein group (young, 0.101±0.008; elderly, 0.113±0.002) (P>0.05). After meal ingestion there was an expected dilution of the labeled plasma phenylalanine pool. Mean postprandial enrichment values in the moderate-protein group (113 g beef) were 0.105±0.002 (young) and 0.105±0.004 (elderly) (P>0.05), whereas enrichment values in the high-protein group (340 g beef) were 0.090±0.008 (young) and 0.092±0.009 (elderly), (P>0.05). As described, a correction factor was applied to account for the transient postprandial decrease in the precursor enrichment and subsequent underestimation of mixed muscle fractional synthesis rate (11).
Protein synthesis after ingestion of 113 g and 340 g lean beef are presented in Figure 2. Postabsorptive mixed muscle FSR values were similar in all groups and did not differ with age. Ingestion of 340 g lean beef increased mixed muscle FSR by approximately 46% (P=0.008) in both the young and the elderly subjects. This was consistent with the 50% increase after ingestion of 113 g lean beef (11). Dose- and age-specific differences were too small to be considered physiologically relevant, particularly if considered in the context of the myriad additional factors that would influence protein synthesis in a real-world setting.
Full-size image (17K)
Figure 2. Mean (±standard error of the mean) mixed muscle fractional synthesis rate before and after ingestions of 113 g (A), or 340 g (B) of 90% lean ground beef by young and elderly subjects. *Significant increase from fasting (young and elderly) after 113 g and 340 g lean beef (P=0.008).
There is little debate that the ingestion of high-quality protein is of paramount importance in the maintenance of muscle mass and function in elderly people. To this end, our findings are consistent with previous work demonstrating an improved protein synthetic response to intact protein sources such as whey protein, milk, and beef ([11], [13], [22] and [23]). However, in circumstances in which the total ingested protein content is low (ie, EAA content less than approximately 7 g) (24) or when glucose and amino acids are co-ingested (25), the protein synthetic response of elders may be blunted compared with the response in their younger counterparts. These findings may have considerable practical significance if they reflect the response to the smaller, mixed-nutrient meals commonly consumed by many older adults.
Although a blunted protein-anabolic response to a small, mixed-nutrient meal may, over time, contribute to the development of sarcopenia (25), there is no age-related discrepancy in muscle protein synthesis after ingestion of a higher total amino acid load ([12], [14], [26] and [27]). In the current study, participants consumed approximately 30 g or 90 g of high-quality protein in a single serving. The key finding was that no further protein synthetic advantage was elicited by the larger meal when compared with the response to a more moderate 30-g protein serving (20). In terms of stimulating muscle growth, it therefore seems likely that under resting/nonexercising conditions, consumption of more than 30 g protein in a single meal is not justified. Indeed, it may well be the case that a slightly smaller meal would produce a similar protein synthetic response.
The data presented in this study represent a practical extension of previous proof-of-concept research that has largely focused on amino acid or whey protein supplementation ([13], [14], [24] and [28]). Nevertheless, there are several limitations that could influence our results. Perhaps the most obvious is the fact that a single menu item, such as a serving of lean beef, is seldom eaten alone. As noted, there are some data suggesting that elders may have a less robust protein synthetic response to the combined ingestion of protein and carbohydrate than their younger counterparts (25). This has yet to be explored in the context of an actual mixed-nutrient meal, but warrants further investigation. Further, there is the potential of an added protein synthetic response if protein were to be consumed in close temporal proximity to physical activity ([29] and [30]).
In summary, a large (340 g) serving of lean beef increases mixed muscle protein synthesis by approximately 50% in both young and elderly subjects. However, a moderate-size portion (113 g) represents an equally effective and more energetically efficient means of stimulating muscle protein synthesis than the threefold larger serving. We suggest that instead of a single, large protein-rich meal, ingestion of multiple moderate-sized servings of high-quality protein-rich foods over the course of a day may represent an effective means of optimizing the potential for muscle growth while permitting greater control over total energy and nutrient intake.
What to take from is more so that increasing protein intake above the 30g was no more effective at muscle synthesis. Muscle developed at the same rate when a 3x larger serving of protein was administered. The limitations are mentioned at the end and yes physical activity is mentioned.
However, 80g of casein being fully absorbed I struggle with that. But until I see proof of that I would stop challenging this claim. You can't fight the science and I will change my beliefs when I see the evidence.
As for the DNA synthesis vs Protein Synthesis. I am mistaken. Parts of what I said were correct and others not. Protein is responsible for structural function which is making all the cells in the body which are protein, so it is protein synthesis. Yes DNA does contain some amino acids, and no protein is not essential for DNA synthesis. I will admit my fault with regards to that and misinterpretation of the facts.
your understanding of DNA, what "building block of life" means and the relationship with amino acids is really suspect. DNA is a blue print for protein synthesis. DNA is made up of nucleic acids, these ARE NOT the same as amino acids. Just because they contain similar atoms (carbon and nitrogen) does not mean they are the same thing.
For 72 hours before admission, participants were asked to maintain their normal diet and avoid strenuous activity. Participants stayed overnight in the General Clinical Research Center and were studied the following morning after an overnight fast. Subjects remained largely physically inactive (ie, rested in bed) for the duration of the study.
The data presented in this study represent a practical extension of previous proof-of-concept research that has largely focused on amino acid or whey protein supplementation ([13], [14], [24] and [28]). Nevertheless, there are several limitations that could influence our results. Perhaps the most obvious is the fact that a single menu item, such as a serving of lean beef, is seldom eaten alone. As noted, there are some data suggesting that elders may have a less robust protein synthetic response to the combined ingestion of protein and carbohydrate than their younger counterparts (25). This has yet to be explored in the context of an actual mixed-nutrient meal, but warrants further investigation. Further, there is the potential of an added protein synthetic response if protein were to be consumed in close temporal proximity to physical activity ([29] and [30]).
I'll say it again, this study is bunk when talking about protein needs of individuals who eat more than just beef during a meal and who actually exercise. Other nutrients consumed during a meal is only irrelevant if you don't want to look at a real world scenario.
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