The nature of the ingested protein has no effect on lean body mass during energy restriction in overweight rats

Severe energy restriction in obesity not only leads to fat mass loss but also to lean mass loss. The aim of this study was to compare the capacity of casein, a slowly digested protein, and milk soluble proteins (MSP; rapidly digested) to limit the loss of lean mass induced by energy restriction. Obesity was first induced in male Wistar rats by a 5-week feeding with a high-fat high-sucrose diet. The impact of energy restriction was then studied with high-protein (32%) diets containing either casein, MSP, or a 50/50 mixture of both proteins for 3 weeks (n = 10 per group). Food intake, body weight, nitrogen balance, creatinine, and 3-methyl-histidine excretion were measured during energy restriction. Then, tissue weights, plasma metabolic parameters (amino acids, glucose, insulin, cholesterol, triglycerides), and in vivo liver and extensor digitorum longus (EDL) muscle protein synthesis rates were measured in postabsorptive state at the end of the experimental period. Although significant differences relevant to protein metabolism were observed between groups (protein intake, plasma amino acid concentrations, fecal nitrogen excretion, muscle protein synthesis rates), week per week, there were no significant differences in nitrogen balance whatever the protein used. In conclusion, our results show that in young overweight energy restricted rats, using a high-protein diet, the nature of protein intake has no influence on body protein retention.     

Cell growth of skeletal muscle as an indicator of protein requirements of the adult rat

Skeletal muscle growth, muscle nucleic acids and muscle protein synthesis capacity, were measured to evaluate the protein requirement of adult rats. Wistar rats were fed on diets containing 4%, 10% or 20% casein + D,L-methionine. All diets were provided for 21 days beginning at 90 days of age. Body weight, food efficiency and net weight change increased as the casein content of the diet increased. Muscle DNA, RNA and RNA/protein were lost, but protein and protein/DNA increased on the 4% and 20% protein diet. This fact involves an aplasia phenomenon although the hypertrophic growth is maintained. Alterations of the insulin and GH plasma levels were observed. These findings indicate that for adult rats the 4% and 20% protein diets are not adequate for the period of adult maintenance.     

Dietary protein levels affect growth and protein metabolism in trunk muscle of cod,Gadus morhua

Summary Cod (Gadus morhua) of 50 g body weight were kept at 14°C. The fish were fed ad libitum during 80 days a diet containing protein levels which in terms of total energy corresponded to 25%, 45% or 65%. Growth increased in accordance with protein-energy levels. The protein content per gram of wet weight of white trunk muscle was unchanged, as was the myofibrillar protein myosin heavy chain determined by the antigen-antibody reaction of the enzyme-linked immunosorbent assay. The amount of messenger ribonucleic acid (mRNA) coding for myosin heavy chain was lower at 25% than at 45% or 65% protein-energy intake, the differences being significant per gram of wet weight of muscle. Acid proteinase activity was highest at the lowest protein-energy intake. Glycogen content in muscle increased with the protein-energy levels. It is concluded that the metabolic response of white trunk muscle to graded protein-energy intake included a change in the capacity to synthesize myosin heavy chain as judged by its mRNA content. The protein content per gram of wet weight was unaffected by dietary protein-energy levels of 25%, 45% and 65%, but protein accretion and thus growth of the animals increased with the protein intake. Dietary protein-energy restriction caused a rise in acid proteinase activity and a decrease in content of mRNA for myosin heavy chain, resulting in a diminished growth rate at an unchanged protein content per gram of wet weight of muscle.Abbreviations CTP cytidine triphosphate - DNA desoxyribonucleic acid - EDTA ethylenediaminetetra-acetic acid - mRNA messenger ribonucleic acid - TRIS tris(hydroxymethyl)aminomethane     

A comparative study of protein synthesis in vitro by skeletal muscle ribosomes from livestock

Skeletal muscle was dissected from the forelimbs of animals and stored at -80 degrees C. Protein synthesis activity was determined in cell-free systems. Incorporation of amino acids into protein was expressed per milligramme of ribosomal RNA, per gramme wet weight of skeletal muscle and per milligramme of DNA. Species related differences in activity were observed in skeletal muscle obtained from pig, horse, lamb, sheep, calf and young steer. Intraspecies differences were seen in cattle of different breeds. The protein composition of the muscle tissue showed quantitative differences between the species. Using biopsy specimens, the system could be used to monitor the protein nutrition status of animals and the production of animal proteins.     

Myofibrillar protein synthesis in myostatin-deficient mice

Either increased protein synthesis or prolonged protein half-life is necessary to support the excessive muscle growth and maintenance of enlarged muscles in myostatin-deficient mice. This issue was addressed by determining in vivo rates of myofibrillar protein synthesis in mice with constitutive myostatin deficiency (Mstn(DeltaE3/DeltaE3)) or normal myostatin expression (Mstn(+/+)) by measuring tracer incorporation after a systemic flooding dose of l-[ring-(2)H(5)]phenylalanine. At 5-6 wk of age, Mstn(DeltaE3/DeltaE3) mice had increased muscle mass (40%), fractional rates of myofibrillar synthesis (14%), and protein synthesis per whole muscle (60%) relative to Mstn(+/+) mice. With maturation, fractional rates of synthesis declined >50% in parallel with decreased DNA and RNA [total, 28S rRNA, and poly(A) RNA] concentrations in muscle. At 6 mo of age, Mstn(DeltaE3/DeltaE3) mice had even greater increases in muscle mass (90%) and myofibrillar synthesis per muscle (85%) relative to Mstn(+/+) mice, but the fractional rate of synthesis was normal. Estimated myofibrillar protein half-life was not affected by myostatin deficiency. Muscle DNA concentrations were reduced in both young and mature Mstn(DeltaE3/DeltaE3) mice, whereas RNA concentrations were normal, so the ratio of RNA to DNA was approximately 30% greater than normal in Mstn(DeltaE3/DeltaE3) mice. Thus the increased protein synthesis and RNA content per muscle in myostatin-deficient mice cannot be explained entirely by an increased number of myonuclei.     

The relationship between protein retention and energy requirements in rats of different ages

Male Wistar rats aged 30, 75 and 150 days were fed for 14 days ad libitum on diets with an optimum protein content (15% for 30-day-old, 12.5% for 75-day-old and 10% for 150-day-old animals) and a mounting fat content (from 5 to 40%), supplemented by saccharides (from 76 to 41%). Net protein utilization was determined for each of the diets from the body nitrogen and protein intake values. Protein retention values were determined from protein intake on the basis of net protein utilization (NPU). Energy intake was computed from fat and saccharide intake, using energy coefficients. The optimum fat content of the diet, evaluated from the maximum protein retention value per day and the minimum amount of energy needed for the retention of 1 g protein, is 30% at 30 days, 15% at 75 days and 10% at 150 days. Protein retention per kg body weight falls with advancing age--mildly at 75 days compared with 30 days, but markedly at 150 days. From their smaller weight increments and NPU values and also from their lower protein retention, 150-day-old animals are characterized by slower growth and higher protein requirements for maintenance of their organism likewise demonstrated by the growth parameter net protein ratio (NPR). Energy requirements for total protein retention/day per kg body weight diminish with age. In old age a small amount of energy is needed only for the maintenance of body functions. This study contributes to the expression of the interrelationship of energy requirements and protein retention.     

Effect of leucine-rich dietary protein on in vitro protein synthesis in porcine muscle

Experiments were conducted to determine the effect of feeding diets containing leucine-rich proteins on in vitro protein synthesis in porcine muscle. Swine (10 kg initial weight) were fed for 4 weeks diets composed mainly of corn gluten meal, corn and soybean meal, and containing a total of 2.00, 2.33, 2.92, 3.12, 3.53, and 4.01% leucine. At the end of the growing period, six swine fed each diet were killed and samples of biceps femoris, longissimus dorsi, and triceps brachii were excised. Incorporation of [14C]phenylalanine into newly synthesized protein was measured using a cell-free in vitro system following recombination of purified soluble protein and ribosomal fractions. The feeding of diets containing increasing amounts of leucine-rich protein increased the free leucine concentration in plasma and skeletal muscle. There was no significant effect of diet on incorporation of [14C]phenylalanine into muscle protein following simple recombination of soluble protein and ribosomal fractions from the same tissues. Combination of muscle soluble protein from animals fed 2.00% leucine with ribosomal fractions of animals fed increasing quantities of leucine-rich protein, however, indicated increased protein synthetic activity of the ribosomal fraction in all muscles tested. Protein synthetic activity of the soluble protein fraction was not affected by diet. It was concluded that the feeding of leucine-rich dietary proteins beyond requirements for maximal rate of growth can increase the protein synthetic potential of porcine muscle cells although whole body growth is depressed.     

Bacterial protein meal in diets for growing pigs: effects on protein and energy metabolism

This experiment investigated the effects of increasing the dietary content of bacterial protein meal (BPM) on the protein and energy metabolism of pigs from weaning to a live weight of 80 kg. Four litters with four castrated male pigs in each litter were used. The litters were divided into two blocks according to age. One pig from each litter was fed one of the four experimental diets. Soya-bean meal was replaced with BPM on the basis of digestible protein, and the BPM contents in the four diets were 0% (BP0), 5% (BP5), 10% (BP10) and 15% (BP15), corresponding to 0%, 17%, 35% and 52% of the digestible nitrogen (N), respectively. Four balance periods were performed, at the start of which the pigs weighed 9.5 kg, 20.7 kg, 45.3 kg and 77.2 kg, respectively. Once during each balance period, 22-h respiration experiments were performed using indirect calorimetry. Daily weight gain, feed intake and feed conversion rate were the same for all diets. The apparent digestibility of N was lower on diet BP10 than on BP0 (P = 0.002), whereas the apparent digestibility of energy was similar on all diets. The retention of nitrogen did not differ between diets and was 1.50, 1.53, 1.33 and 1.46 g N per kg^0.75 per day on BP0, BP5, BP10 and BP15, respectively. Neither metabolisable energy intake nor heat production were affected by inclusion level of BPM. Retention of energy was 620 (BP0), 696 (BP5), 613 (BP10) and 664 kJ/kg^0.75 per day (BP15), the differences among diets being non-significant. The N-free respiratory quotient was similar on all diets. It was concluded that the overall protein and energy metabolism in growing pigs were not affected when up to 50% of dietary N was derived from BPM.     

Effect of dietary lysine on muscle protein turnover in growing chickens.

Day-old male chickens were fed ad libitum isoenergetic diets containing 20% crude protein but differing in their lysine content (from 6.5 up to 11.3 g/kg). At 3 weeks of age, protein fractional synthesis rates in the pectoralis major muscle were determined using a large dose injection of 120 mumol per kg body weight of L-[4-3H] phenylalanine. Protein gain in the pectoralis major was measured between 19 and 23 days of age. Protein breakdown was obtained by calculating the difference between protein synthesis and deposition. Weight gain varied curvilinearly with dietary lysine intake and was maximum for 11.3 g lysine/kg of diet. In birds fed an adequate lysine intake (10.1-11.3 g/kg) protein fractional synthesis and breakdown rates were 23.6-25.9 and 17.8-19.8%/d respectively. Increasing lysine supplementation in the diet resulted in an impairment of protein fractional breakdown rates. By contrast, protein fractional synthesis rates remained unchanged owing mainly to an improvement in the synthesis efficiency (kRNA), until birds were fed an adequate lysine intake. These data suggest that the growth rate reduction of chickens fed lysine deficient diets was due to alterations in both rates of protein synthesis and breakdown in skeletal muscle. A maximum protein deposition is achieved when kRNA was optimal, ie for a dietary lysine content of about 9 g/kg, a value close to the requirement.     

Protein metabolism in the small intestine of the ethanol-fed rat

The effects of chronic ethanol feeding on the small intestine were investigated in young rats. Rats were fed a nutritionally-adequate liquid diet, containing 36 per cent of total energy as ethanol (treated, n = 7), or isovolumetric amounts of the same diet in which ethanol was substituted by isocaloric glucose (controls, n = 7). After six weeks the wet weight and total tissue contents of protein, RNA and DNA were significantly reduced by 21 per cent, 23 per cent, 16 per cent and 28 per cent respectively, (p less than 0.014). Rates of protein synthesis were measured with L[4(3H)]phenylalanine and fractional rates (defined as the percentage of constituent tissue protein synthesised each hour, i.e. ks, % h-1) were calculated from the specific radioactivity of free phenylalanine in both tissue homogenates and plasma. Ethanol-feeding reduced ks by approx 10 per cent (p less than 0.181). The amount of protein synthesized unit-1 RNA was also reduced by approx 15 per cent (p less than 0.059) but the amount of protein synthesis unit-1 DNA was unaffected by ethanol-feeding (p less than 1.000). In contrast, the absolute rates of protein synthesis were reduced by approximately 30 per cent (p less than 0.022). It was concluded that, as the small intestine contributes to approx. 20-25 per cent of whole body synthesis these results may have an important effect on whole body nitrogen homeostasis and may have implications for the gastrointestinal effects of ethanol seen during chronic alcoholic abuse.     

Growth and muscle protein turnover in the chick

The growth rates of young chicks were varied from 0 to 10% per day by manipulation of the adequacy of the amino acid and energy supply. The rates of protein synthesis in the white breast (pectoralis thoracica) muscle and the dark leg (gastrocnemius and peronaeus longus) muscles were estimated by feeding l-[U-¹⁴C]tyrosine in amino acid/agar-gel diets (`dietary infusion'). This treatment rapidly and consistently produced an isotopic equilibrium in the expired CO₂ and in the free tyrosine of plasma and the muscles. Wholebody protein synthesis in 2-week-old chicks was estimated from the tyrosine flux and was 6.4g/day per 100g body wt. In 1-week-old chicks the rate of protein synthesis was more rapid in the breast muscles than in the leg muscles, but decreased until the rates were similar in 2-week-old birds. Synthesis was also more rapid in fast-growing Rock Cornish broilers than in medium-slow-growing New Hampshire×Single Comb White Leghorn chicks. No or barely significant decrease in the high rates of protein synthesis, in the protein/RNA ratio and in the activity of RNA for protein synthesis occurred in non- or slow-growing chicks fed on diets deficient in lysine, total nitrogen or energy. Thus the machinery of protein synthesis in the young chick seems to be relatively insensitive to dietary manipulation. In the leg muscles, there was a small but significant correlation between the fractional rate of growth and protein synthesis. A decrease in the fractional rate of degradation, however, appeared to account for much of the accumulation of muscle protein in rapidly growing birds. In addition, the rapid accumulation of breast-muscle protein in rapidly growing chicks appeared to be achieved almost entirely by a marked decrease in the fractional rate of degradation.     

Protein and RNA synthesis in the skeletal muscle of hereditary dystrophic mouse.

Protein and RNA contents in muscle of normal and hereditary dystrophic mice C57BL/6J-dy/dy were reexamined on the basis of DNA. It was observed that protein and RNA contents in dystrophic muscle decreased at the early stage of the disease, in disagreement with the reported results on a wet weight basis, in which RNA content in dystrophic muscle had been found to increase. Rates of protein and RNA systhesis in the early stage of the disease were also determined with a concomitant check of the specific activities of free amino acids and free nucleotides. The rates of both protein and RNA synthesis (i.e., specific activities of protein and RNA) were higher in the dystrophic muscle, but when they were expressed on a DNA basis, the total protein synthesis per cell was the same as that of normal muscle and the total RNA synthesis per cell showed a smaller increase in dystrophic muscle. These apparent increases of protein and RNA synthesis were discussed in connection with the decreased protein and RNA contents in the cells of dystrophic muscle. The synthesized RNAs seemed to contain mRNA on the basis of sedimentation character and Millipore filter binding ability. However, no particular RNA was mainly synthesized in dystrophic muscle.     

Muscle cell growth in protein deficient rats following administration of sheep red blood cells.

In order to observe the effects of sheep red blood cells (SRBC) administration on the muscle cell growth in malnourished states, adult male Wistar rats (135 +/- 10 g 10 animals per group) subjected during 30 days to 1% and 10% protein diets, were injected (i.v.) either 15.5 x 10(8) sheep red blood cells or 0.5 ml saline/100 g b.w. after 20 days of experiment. On the 10th day after injection the animals were sacrificed and the gastrocnemius muscle was removed, weighed and homogenized. The supernatant fluids were used to evaluate muscle protein, DNA and RNA rates and acid DNase activity. All parameters were depleted in malnourished rats, indicating a muscle cellular atrophy as well as a decrease in muscle protein synthesis per DNA-unit. Muscle hyperplasia and hypertrophy were found in antigenically stimulated rats fed 10% protein against non-stimulated control. In contrast, muscle growth in protein-deficient rats SRBC-treated was unmodified when compared to non-stimulated malnourished muscle, although RNA functionality seems to be enhanced (RNA/DNA). These data suggest that a redistribution of essential nutrients occurred for muscle growth adaptation rather than for defensive mechanism.     

The effect of chronic ethanol ingestion on protein metabolism in type-I- and type-II-fibre-rich skeletal muscles of the rat.

1. The effects of chronic ethanol feeding on muscles containing a predominance of either Type I (aerobic, slow-twitch) or Type II (anaerobic, fast-twitch) fibres were studied. Male Wistar rats, weighing approx. 90 g or 280 g, were pair-fed on a nutritionally complete liquid diet containing 36% of total energy as ethanol, or isovolumetric amounts of the same diet in which ethanol was replaced by isoenergetic glucose. After 6 weeks feeding, fractional rates of protein synthesis were measured with a flooding dose of L-[4-(3)H]-phenylalanine and muscles were analysed for protein, RNA and DNA. 2. Ethanol feeding decreased muscle weight, protein, RNA and DNA contents in both small and large rats. Type-II-fibre-rich muscles showed greater changes than did Type-I-fibre-rich muscles. Changes in protein paralleled decreases in DNA. 3. The capacity for protein synthesis (RNA/protein), fractional rates of protein synthesis and absolute rates of protein synthesis were decreased by ethanol feeding in both small and large rats. The amounts of protein synthesized relative to RNA and DNA were also decreased. Changes were less marked in Type-I than in Type-II-fibre-rich muscles. Loss of protein, RNA and DNA was greater in small rats, but protein synthesis was more markedly affected in large rats. 4. It was concluded that chronic ethanol feeding adversely affects protein metabolism in skeletal muscle. Fibre composition and animal size are also important factors in determining the pattern of response.     

Dietary protein regulates hepatic constitutive protein anabolism in rats in a dose-dependent manner and independently of energy nutrient composition

We had previously observed that drastic increases in protein consumption greatly modified hepatic protein anabolism in rats, but the confounding effects of other macronutrient changes or a moderate protein increase to generate the same modifications have not yet been established. This study examined the metabolic and hormonal responses of rats subjected to 14-day isoenergetic diets containing normal, intermediate, or high-protein levels (NP: 14% of energy, IP: 33%, HP: 50%) and different carbohydrate (CHO) to fat ratios within each protein level. Fasted or fed rats (n = 104) were killed after the injection of a flooding dose of (13)C-valine. The hepatic protein content increased in line with the dietary protein level (P < 0.05). The hepatic fractional synthesis rates (FSR) of protein were significantly influenced by both the protein level and the nutritional state (fasted vs. fed) (P < 0.0001) but not by the CHO level, reaching on average 110%/day, 92%/day, and 83%/day in rats fed the NP, IP, and HP diets, respectively. The FSR of plasma albumin and muscle did not differ between diets, while feeding tended to increase muscle FSR. Proteolysis, especially the proteasome-dependent system, was down-regulated in the fed state in the liver when protein content increased. Insulin decreased with the CHO level in the diet. Our results reveal that excess dietary protein lowers hepatic constitutive, but not exported, protein synthesis rates, independently of the other macronutrients, and related changes in insulin levels. This response was observed at the moderate levels of protein intake (33%) that are plausible in a context of human consumption.     

Pre- and post-natal growth and protein turnover in smooth muscle, heart and slow- and fast-twitch skeletal muscles of the rat.

The growth of one smooth and three individual striated muscles was studied from birth to old age (105 weeks), and where possible during the later stages of foetal life also. Developmental changes in protein turnover (measured in vivo) were related to the changing patterns of growth within each muscle, and the body as a whole. Developmental growth (i.e. protein accumulation) in all muscles involved an increasing proportion of protein per unit wet weight, as well as cellular hypertrophy. The contribution of the heart towards whole-body protein and nucleic acid contents progressively decreased from 18 days of gestation to senility. In contrast, post-natal changes in both slow-twitch (soleus) and fast-twitch (tibialis anterior) skeletal muscles remained reasonably constant with respect to whole-body values. Such age-related growth in all four muscle types was accompanied by a progressive decline in both the fractional rates of protein synthesis and breakdown, the changes in synthesis being more pronounced. Age for age, the fractional rates of synthesis were highest in the oesophageal smooth muscle, similar in both cardiac and the slow-twitch muscles, and lowest in the fast-twitch tibialis muscle. Despite these differences, the developmental fall in synthetic rates was remarkably similar in all four muscles, e.g. the rates at 105 weeks were 30-35% of their values at weaning. Such developmental changes in synthesis were largely related to diminishing ribosomal capacities within each muscle. When measured under near-steady-state conditions (i.e. 105 weeks of age), the half-lives of mixed muscle proteins were 5.1, 10.4, 12.1 and 18.3 days for the smooth, cardiac, soleus and tibialis muscles respectively. Old-age atrophy was evident in the senile animals, this being more marked in each of the four muscle types than in the animal as a whole. In each muscle of the senile rats the protein content and composition per unit wet weight, and both the fractional and total rates of synthesis, were significantly lower than in the muscles of younger, mature, animals (i.e. 44 weeks). In the soleus the decreased synthesis rate appeared to be related to a further fall in the ribosomal capacity. In contrast, the changes in synthesis in the three remaining muscles correlated with significant decreases in the synthetic rate per ribosome.(ABSTRACT TRUNCATED AT 400 WORDS)     

Changes in the metabolism of muscle RNA in rats given a high protein diet

The effect of a high protein diet (20% casein + D,L-methionine) administered to adult Wistar rats on some aspects of muscle RNA metabolism has been studied. Body weight increased in spite of lower intake. However, gastrocnemius muscle remained unmodified, although protein content increased. Total RNA decreased in the whole muscle although RNA/DNA ratio did not change. Protein synthesis capacity diminished 81% relative to controls in spite the fact that an excessive amount of available amino acids exists. RNA loss might depend on a high catabolism, since acid RNase activity increased over control values. Therefore, it may be concluded that a high protein diet leads to a lower protein synthesis capacity through an elevated RNA breakdown.     

Short-term, increasing dietary protein and fat moderately affect energy expenditure, substrate oxidation and uncoupling protein gene expression in rats

Macronutrient composition of diets can influence body-weight development and energy balance. We studied the short-term effects of high-protein (HP) and/or high-fat (HF) diets on energy expenditure (EE) and uncoupling protein (UCP1-3) gene expression. Adult male rats were fed ad libitum with diets containing different protein-fat ratios: adequate protein-normal fat (AP-NF): 20% casein, 5% fat; adequate protein-high fat (AP-HF): 20% casein, 17% fat; high protein-normal fat (HP-NF): 60% casein, 5% fat; high protein-high fat (HP-HF): 60% casein, 17% fat. Wheat starch was used for adjustment of energy content. After 4 days, overnight EE and oxygen consumption, as measured by indirect calorimetry, were higher and body-weight gain was lower in rats fed with HP diets as compared with rats fed diets with adequate protein content (P<.05). Exchanging carbohydrates by protein increased fat oxidation in HF diet fed groups. The UCP1 mRNA expression in brown adipose tissue was not significantly different in HP diet fed groups as compared with AP diet fed groups. Expression of different homologues of UCPs positively correlated with nighttime oxygen consumption and EE. Moreover, dietary protein and fat distinctly influenced liver UCP2 and skeletal muscle UCP3 mRNA expressions. These findings demonstrated that a 4-day ad libitum high dietary protein exposure influences energy balance in rats. A function of UCPs in energy balance and dissipating food energy was suggested. Future experiments are focused on the regulation of UCP gene expression by dietary protein, which could be important for body-weight management.     

Turnover of muscle protein in the fowl (Gallus domesticus). Rates of protein synthesis in fast and slow skeletal, cardiac and smooth muscle of the adult fowl.

Rates of protein synthesis in skeletal, cardiac and smooth muscle of fully grown fowl (Gallus domesticus) were determined in vivo by means of the constant infusion method using [14C]proline. In the anterior latissimus dorsi muscle, containing predominantly slow fibres, the average synthesis rate of non-collagen muscle proteins was 17.0 +/- 3.1% per day, a value higher than that obtained for cardiac muscle (13.8 +/- 1.3% per day) and for smooth muscle of the gizzard (12.0 +/- 1.9% per day). In the posterior latissimus dorsi muscle, containing predominantly fast fibres, synthesis rates were much lower (6.9 +/- 1.8% per day). In each case these average rates for the non-collagen protein were similar to the average rate for the sarcoplasmic and myofibrillar protein fractions. The RNA concentration of these four muscles showed that relative rates of protein synthesis were determined mainly by the relative RNA concentrations. The rate of protein synthesis per unit of DNA (the DNA activity) was similar in the two skeletal muscles, but somewhat lower in cardiac muscle and gizzard, possibly reflecting the larger proportion of less active cell types in these two muscles. These quantitative aspects of protein turnover in the two skeletal muscles are discussed in terms of the determination of ultimate size of the DNA unit, and in relation to muscle ultrastructure.     

Quantitative protein requirements of Arctic charr, Salvelinus alpinus (L)

Arctic charr, Salvelinus alpinus , require diets with protein energy (PE): total energy (TE) ratios of at least 0.35 in order to maintain good rates of growth. The protein requirement is, therefore, similar to that of rainbow trout, Salmo gairdneri . Protein retention efficiency (PPV) declined as the protein content of the diet was increased, the relationship being described by the equation: It is suggested that charr will maintain good rates of growth if fed on diets used for commercial culture of rainbow trout and special formulations for charr should not be necessary.