scholarly journals Allometric growth of protein, amino acids, fat and minerals in slow- and fast-growing young chickens

2011 ◽  
Vol 56 (No. 3) ◽  
pp. 127-135 ◽  
Author(s):  
J. Zelenka ◽  
J. Heger ◽  
S. Kráčmar ◽  
E. Mrkvicová
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nitrogen Retention ◽  
Growth Period ◽  
The Body ◽  
Allometric Growth ◽  
Retention Efficiency ◽  
Body Protein ◽  
Fast Growing ◽  
Protein Amino Acids

Allometric growth of body constituents and apparent efficiency of amino acid and nitrogen retention were examined in slow-growing laying-type cockerels (SG) and in fast-growing male broiler hybrids (FG) during the growth period from hatch to Day 22. The respective allometric coefficients for water, protein, (N × 6.25)ash and fat in relation to body weight were 0.971, 1.080, 1.096 and 1.284 for SG chickens and 0.977, 1.099, 0.993, and 1.198 for FG chickens. The respective allometric coefficients describing the relationships of water, fat and ash weight with protein weight were 0.894, 1.014, and 1.186 for SG chickens and 0.893, 0.910, and 1.097 for FG chickens. High allometric coefficients for ash in both genotypes likely indicate the rapid growth of skeletal tissues which requires adequate mineral nutrition during this period of growth. The deposition of ash relative to protein was significantly higher (P < 0.05) in SG chickens thus suggesting that the relative growth of ash may be affected by genotype. Allometric coefficients relating amino acids to body protein were less than unity in most cases which indicates that an increasing amount of non-protein N is deposited in the body with advancing age. Except for cysteine, the apparent efficiency of amino acid retention was lower in SG as compared to FG chickens. The high retention efficiency of cysteine in SG genotype was likely associated with the conversion of surplus methionine to cysteine, required for feather protein synthesis in laying-type birds at an early age.

scholarly journals HEMOGLOBIN AND PLASMA PROTEIN

1943 ◽  
Vol 77 (4) ◽  
pp. 375-396 ◽  
Author(s):  
F. S. Robscheit-Robbins ◽  
L. L. Miller ◽  
G. H. Whipple
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Plasma Protein ◽  
The Body ◽  
Acid Mixture ◽  
Blood Proteins ◽  
Body Protein ◽  
Growth Mixture ◽  
Amino Acid Mixtures ◽  
Hemoglobin Production

Given healthy dogs, fed abundant iron and protein-free or low protein diets, with sustained anemia due to bleeding, we can study the capacity of these animals to produce simultaneously new hemoglobin and plasma protein. The reserve stores of blood protein producing materials in this way are very largely depleted, and levels of 6 to 8 gm. per cent for hemoglobin and 4 to 5 gm. per cent for plasma protein can be maintained for considerable periods of time. These dogs are very susceptible to infection and to injury by many poisons. Under such conditions, these anemic and hypoproteinemic dogs will use very efficiently a variety of digests (serum, hemoglobin, and casein) and the growth mixture (Rose) of pure amino acids. Nitrogen balance is maintained and considerable new blood proteins are produced. Dog plasma by vein is used freely in these doubly depleted dogs to make new hemoglobin in abundance (Table 1). Serum digests by vein are well utilized to make new hemoglobin and plasma protein in the same dogs (Table 1). Serum digests by mouth are effectively used to make new blood proteins (Table 5). Dog or sheep hemoglobin given in large amounts intraperitoneally are remarkably well utilized to form hemoglobin and plasma protein (Table 6). It must be obvious that the globin of the hemoglobin is saved in these protein-depleted dogs and used to make large amounts of hemoglobin and plasma protein. Hemoglobin digests are also well utilized whether given by mouth (Table 7) or by vein (Table 8) and liberal amounts of plasma protein are manufactured from digests presumably ideally suited for hemoglobin production. Casein digests are well used (Table 8) and form as much new plasma protein as any material tested—even serum digests. Amino acid mixtures are of especial interest. The growth mixture of 10 amino acids (Rose) is well utilized by mouth or by vein and favors new hemoglobin production more than any material tested (Table 2). Cystine replacing methionine in the amino acid mixture increases the plasma protein—hemoglobin output ratio, that is it favors plasma protein production. Digests of various sorts and amino acid mixtures or combinations of digests and amino acid mixtures can be used rapidly and effectively to build new hemoglobin or plasma protein, to maintain nitrogen equilibrium, and to replete reserve protein stores. These experiments point to clinical problems. The unexplained preference given to hemoglobin production in these hypoproteinemic dogs is observed under all conditions, even when whole plasma or serum digests are given by vein. In general, 2 to 4 gm. of hemoglobin are formed for every gram of plasma protein. This all adds up to a remarkable fluidity in the use of plasma protein or hemoglobin which can contribute directly to the body protein pool from which are evolved, without waste of nitrogen, the needed proteins, whether hemoglobin, plasma protein, or tissue proteins.

scholarly journals Methionine plus cystine to lysine ratio in diets for tambatinga fingerlings

2021 ◽  
Vol 45 ◽  
Author(s):  
Dayana da Conceição da Costa ◽  
Marcos Antonio Delmondes Bomfim ◽  
Felipe Barbosa Ribeiro ◽  
Jefferson Costa de Siqueira ◽  
Neliane Galvão Porto ◽  
...  
Keyword(s):  
Weight Gain ◽  
Amino Acid ◽  
Nitrogen Retention ◽  
Feed Conversion ◽  
Rapid Weight Gain ◽  
Retention Efficiency ◽  
Body Protein ◽  
Protein Deposition ◽  
Amino Acid Requirements ◽  
Amino Acid Methionine

ABSTRACT Among a variety of hybrids produced in Brazil, tambatinga is obtained from the crossing of a tambaqui female with a pirapitinga male. Although rapid weight gain in less time is an attractive characteristic from a commercial viewpoint, the information on its nutritional requirements, especially amino acid requirements, is limited. As corn and soybean meal-based diets available for fish contain deficient levels of essential amino acid methionine, our objective was to determine the digestible methionine plus cystine to lysine ratio in diets for tambatinga fingerlings. We used 900 fish with initial weights varying from 1.49 ±0.59 to 4.14 ±1.70 g, and they were fed six types of diets with different digestible methionine plus cystine to lysine ratios (50, 55, 60, 65, 70, and 75%). Performance parameters such as food efficiency, body depositions of protein, fat, and ash, and nitrogen retention efficiency were evaluated. The increase of digestible methionine plus cystine to lysine ratio in the diet improved quadraticly the feed intake, consumption of digestible methionine plus cystine, weight gain, specific growth rate and feed conversion, protein deposition and body ash and retention efficiency nitrogen until the estimated ratios of 57%, 73%, 58%, 58% and 59%, 59%, 58% and 60%, respectively; and reduced linearly the efficiency of using methionine plus cystine for the weight gain. On the other hand, body fat deposition was not affected. We concluded that the digestible methionine plus cystine: lysine ratio in the rations for tambatinga fingerlings is 59%, for provide better performance and body protein deposition.

scholarly journals BIOSYNTHESIS IN ISOLATED ACETABULARIA CHLOROPLASTS

1972 ◽  
Vol 54 (2) ◽  
pp. 279-294 ◽  
Author(s):  
David C. Shephard ◽  
Wendy B. Levin
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Technical Problems ◽  
Hydrolyzed Protein ◽  
Protein Amino Acids ◽  
Amino Acid Labeling ◽  
Labeling Pattern

The ability of chloroplasts isolated from Acetabulana mediterranea to synthesize the protein amino acids has been investigated. When this chloroplast isolate was presented with 14CO2 for periods of 6–8 hr, tracer was found in essentially all amino acid species of their hydrolyzed protein Phenylalanine labeling was not detected, probably due to technical problems, and hydroxyproline labeling was not tested for The incorporation of 14CO2 into the amino acids is driven by light and, as indicated by the amount of radioactivity lost during ninhydrin decarboxylation on the chromatograms, the amino acids appear to be uniformly labeled. The amino acid labeling pattern of the isolate is similar to that found in plastids labeled with 14CO2 in vivo. The chloroplast isolate did not utilize detectable amounts of externally supplied amino acids in light or, with added adenosine triphosphate (ATP), in darkness. It is concluded that these chloroplasts are a tight cytoplasmic compartment that is independent in supplying the amino acids used for its own protein synthesis. These results are discussed in terms of the role of contaminants in the observed synthesis, the "normalcy" of Acetabularia chloroplasts, the synthetic pathways for amino acids in plastids, and the implications of these observations for cell compartmentation and chloroplast autonomy.

Inter-annual and seasonal dynamics of amino acid, mineral and vitamin composition of silver belly Leiognathus splendens

2014 ◽  
Vol 95 (4) ◽  
pp. 817-828 ◽  
Author(s):  
Kajal Chakraborty ◽  
Deepu Joseph
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Content ◽  
West Coast ◽  
Sensor Data ◽  
The South ◽  
Post Monsoon ◽  
South West ◽  
South West Coast ◽  
Protein Amino Acids

Silver bellies, Leiognathus splendens were studied for their spatial (south-west and south-east coasts of India), annual (2008–2011) and seasonal (pre-monsoon, monsoon and post-monsoon) variations of protein, amino acids, vitamins and minerals. The monthly mean Sea Viewing Wide Field-of-view Sensor data for the period from January 2008 to December 2011 were taken into account to indicate the distribution of the photosynthetic pigment chlorophyll-a to test the hypothesis that surface productivity might be related to nutritional biochemistry of this species. The four year average total protein content and chlorophyll-a showed good correlation during monsoon on the south-west coast and monsoon/post-monsoon on the south-east coast, suggesting that the protein content is prejudiced by the chlorophyll-a concentration. Amino acid scores observed monsoon maxima along the south-west and south-east coasts. Significant seasonal variations in vitamin content were observed at the study locations with high content of vitamins D3, E, K1 and C on the south-west coast. Na content was maximal during pre-monsoon on the south-west coast, while post-monsoon maxima of Ca and K content were observed. The Fe, Mn and Zn were abundant in the samples collected from the south-west coast. The concentration of Se exhibited maximum values post-monsoon along the south-west and south-east coasts. The present study demonstrated L. splendens as a valuable source of the protein, amino acids, minerals and vitamins, showing that this low-value species is a good source of well balanced proteins with high biological value to be qualified as a preferred healthy food for human consumption.

THE PROTEOLYTIC ACTIVITY OF INSULIN

1967 ◽  
Vol 45 (9) ◽  
pp. 1329-1333
Author(s):  
Michel Page ◽  
Claude Godin
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Proteolytic Activity ◽  
Protein Amino Acids

The action of insulin on hemoglobin at pH 7.5 was studied. Four different methods were used to determine the degree of proteolysis. After mixtures of hemoglobin and insulin were incubated for 2 hours, very little amino acid or peptide material was liberated from the proteins. As many amino acids are liberated from hemoglobin when it is incubated alone under the same conditions. It is concluded that autolysis is responsible for the observed increases in non-protein amino acids and that insulin has no proteolytic activity under the conditions used in this study.

Amino acids in blood plasma and tissues of rats following glucose force-feeding

1969 ◽  
Vol 47 (3) ◽  
pp. 323-327 ◽  
Author(s):  
J. E. Knipfel ◽  
H. G. Botting ◽  
F. J. Noel ◽  
J. M. McLaughlan
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Blood Plasma ◽  
Protein Composition ◽  
Tissue Uptake ◽  
Body Protein ◽  
Glucose Administration ◽  
Force Feeding ◽  
Amino Acid Requirements ◽  
Concentration Changes

Changes in plasma amino acid (PAA) concentrations effected by force-feeding glucose to rats were studied in two experiments. Attempts were made to relate PAA concentration changes to amino acid requirements, previous diet, time after feeding glucose, and composition of several body proteins. Distribution of 14C-lysine between blood and tissues was examined in an additional rat experiment. Previous diet did not affect the relative quantities of amino acids removed from plasma (PAA removal pattern) after glucose force-feeding. Minimal PAA concentrations occurred by 40 min after glucose administration. The PAA removal pattern was not distinctly related to either amino acid requirements or to any particular body protein composition. Results of administering 14C-lysine simultaneously with glucose indicated that decreased plasma 14C-lysine levels were caused by increased tissue uptake of 14C, likely mediated by insulin. Muscle acted as the major recipient of 14C from plasma, with liver a lesser and more dynamic reservoir of 14C accumulation. Work is continuing to further clarify the significance of the PAA removal pattern, caused by the force-feeding of glucose.

scholarly journals Unusual Aggregation Properties of Single Amino Acid L-Lysine Hydrochloride

2021 ◽  
Author(s):  
Bharti Koshti ◽  
Ramesh Singh ◽  
Vivekshinh Kshtriya ◽  
Shanka Walia ◽  
Dhiraj Bhatia ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Self Assembly ◽  
Short Term Memory ◽  
Deionized Water ◽  
The Body ◽  
The Self ◽  
Single Amino Acid ◽  
Maple Syrup ◽  
Self Assembling

<p>.<br></p><p>The self-assembly of single amino acids is very important topic of research since there are plethora of diseases like phenylketonuria, tyrosinemia, hypertryptophanemia, hyperglycinemia, cystinuria and maple syrup urine disease to name a few which are caused by the accumulation or excess of amino acids. These are in-born errors of metabolisms (IEM’s) which are caused due to the deficiency of enzymes involved in catabolic pathways of these enzymes. Hence, it is very pertinent to understand the fate of these excess amino acids in the body and their self-assembling behaviour at molecular level. From the previous literature reports it may be surmised that the single amino acids like Phenylalanine, Tyrosine, Tryptophan, Cysteine and Methionine assemble to amyloid like structures, and hence have important implications in the pathophysiology of IEM’s like phenylketonuria, tyrosinemia, hypertryptophanemia, cystinuria and hypermethioninemia respectively. In this manuscript we report the self-assembly of lysine hydrocholride to fiber like structures in deionized water. It could be observed that lysine assemble to globular structures in fresh condition and then gradually changes to fiber like morphologies by self-association over time after 24 hours. These fibers gradually change to tubular morphologies after 3 day followed by fractal irregular morphologies in 10 and 15 days respectively. Notably, lysine exists as positively charged amino acid at physiological pH and the amine groups in lysine remain protonated. Hence, the self-assembling properties of lysine hydrochloride in deionized water is also pertinent and give insights into the fate of this amino acid in body in case it remains unmetabolized. Further, MTT assays were done to analyse the toxicities of these aggregates and the assay suggest their cytotoxic nature on SHSY5Y neural cell lines. Hence, the aggregation of lysine may be attributed to the pathological symptoms caused in diseases like hyperlysinemia which is associated with the neurological problems like seizures and short-term memory as observed in case of amyloid diseases like Parkinson’s and Alzheimer’s to name a few.</p>

Nitrogen Homoeostasis in man: Influence of Protein Intake on the Amplitude of Diurnal Cycling of Body Nitrogen

1994 ◽  
Vol 86 (1) ◽  
pp. 91-102 ◽  
Author(s):  
Gill M. Price ◽  
David Halliday ◽  
Paul J. Pacy ◽  
Marcelo R. Quevedo ◽  
D. Joe Millward
Keyword(s):  
Amino Acid ◽  
Protein Intake ◽  
The Body ◽  
N Balance ◽  
N Losses ◽  
Body Protein ◽  
Fed State ◽  
Excretion Rates ◽  
Amino Acid Balance ◽  
Diurnal Cycling

1. The diurnal nature of nitrogen (N) homoeostasis was investigated in adults fed increasing protein intakes. N balance was estimated during a 48 h period of consecutive 12 h periods of feeding hourly meals and fasting, after 12 days of adaptation to diets containing 0.36 +0.01, 0.77 + 0.03, 1.59 +0.08 and 2.31 +0.65 g of protein day−1 kg−1. N losses were determined from measured urinary N excretion corrected for changes in the body urea pool, and estimated faecal and miscellaneous losses. [13C] Leucine and [2H5]phenylalanine balances were measured during a primed, continuous infusion of the two amino acids during the fasting and feeding phase on the second day. 2. Increasing fasting N losses were observed (47 +7, 60+6, 95+15 and 140+36 mg day−1 kg−1) on the four intakes, with corresponding increasing fed gains of 8.2+3.9, 40.2+7.1, 112+24 and 180+ 56 mg day−1 kg−1. 3. Increasing fed-state amino acid gains with increasing protein intake were observed with both [13C]leucine and [2H5]phenylalanine, whereas increasing fasting amino acid losses were confirmed with [13C]leucine. 4. The N equivalent of the leucine oxidation rate was mostly in the range of 10–50% lower than expected from the N excretion rates. This may reflect the timing of the amino acid balance measurements and non-uniform rates of gain and loss throughout the diurnal cycle. 5. We conclude on the basis of both N and amino acid balances that the amplitude of the diurnal cycling of body protein N in human adults increases with increasing dietary protein intake. Thus one component of the protein requirement for N balance reflects a demand for repletion of fasting losses which increases with increasing habitual protein intake.

Consistency and Change

2019 ◽  
Author(s):  
Alan Kelly
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Living Organism ◽  
Peptide Bond ◽  
The Body ◽  
Blood Proteins ◽  
Genes Encoding ◽  
Fundamental Phenomenon ◽  
P Proteins

Proteins are, in my view, the most impressive molecules in food. They influence the texture, crunch, chew, flow, color, flavor, and nutritional quality of food. Not only that, but they can radically change their properties and how they behave depending on the environment and, critically for food, in response to processes like heating. Even when broken down into smaller components they are important, for example giving cheese many of its critical flavor notes. Indeed, I would argue that perhaps the most fundamental phenomenon we encounter in cooking or processing food is the denaturation of proteins, as will be explained shortly. Beyond food, the value of proteins and their properties is widespread across biology. Many of the most significant molecules in our body and that of any living organism (including plants and animals) are proteins. These include those that make hair and skin what they are, as well as the hemoglobin that transports oxygen around the body in our blood. Proteins are built from amino acids, a family of 20 closely related small molecules, which all have in chemical terms the same two ends (chemically speaking, an amino end and an acidic end, hence the name) but differ in the middle. This bit in the middle varies from amino acid to amino acid, from simple (a hydrogen atom in the case of glycine, the simplest amino acid) to much more complex structures. Amino acids can link up very neatly, as the amino end of one can form a bond (called a peptide bond) with the acid end of another, and so forth, so that chains of amino acids are formed that, when big enough (more than a few dozen amino acids), we call proteins. Our bodies produce thousands of proteins for different functions, and the instructions for which amino acids combine to make which proteins are essentially what the genetic code encrypted in our DNA specifies. We hear a lot about our genes encoding the secrets of life, but what that code spells is basically P-R-O-T-E-I-N. Yes, these are very important molecules!

scholarly journals Nonessential amino acid usage for protein replenishment in humans: a method of estimation

2019 ◽  
Vol 110 (2) ◽  
pp. 255-264 ◽  
Author(s):  
Paolo Tessari
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Quality ◽  
Essential Amino Acids ◽  
World Health ◽  
Whole Body ◽  
Published Data ◽  
Total Proteins ◽  
Body Protein ◽  
Amino Acid Turnover

ABSTRACT Background Essential amino acids (EAAs) are key factors in determining dietary protein quality. Their RDAs have been estimated. However, although nonessential amino acids (NEAAs) are utilized for protein synthesis too, no estimates of their usage for body protein replenishment have been proposed so far. Objective The aim of this study was to provide minimum, approximate estimates of NEAA usage for body protein replenishment/conservation in humans. Methods A correlation between the pattern of both EAAs and NEAAs in body proteins, and their usage, was assumed. In order to reconstruct an “average” amino acid pattern/composition of total body proteins (as grams of amino acid per gram of protein), published data of relevant human organs/tissues (skeletal muscle, liver, kidney, gut, and collagen, making up ∼74% of total proteins) were retrieved. The (unknown) amino acid composition of residual proteins (∼26% of total proteins) was assumed to be the same as for the sum of the aforementioned organs excluding collagen. Using international EAA RDA values, an average ratio of EAA RDA to the calculated whole-body EAA composition was derived. This ratio was then used to back-calculate NEAA usage for protein replenishment. The data were calculated also using estimated organ/tissue amino acid turnover. Results The individual ratios of World Health Organization/Food and Agriculture Organization/United Nations University RDA to EAA content ranged between 1.35 (phenylalanine + tyrosine) and 3.68 (leucine), with a mean ± SD value of 2.72 ± 0.81. In a reference 70-kg subject, calculated NEAA usage for body protein replenishment ranged from 0.73 g/d for asparagine to 3.61 g/d for proline. Use of amino acid turnover data yielded similar results. Total NEAA usage for body protein replenishment was ∼19 g/d (45% of total NEAA intake), whereas ∼24 g/d was used for other routes. Conclusion This method may provide indirect minimum estimates of the usage of NEAAs for body protein replacement in humans.

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