scholarly journals Dietetic ingredients of small animals suffering from obesity and their biological role

2018 ◽  
Vol 20 (92) ◽  
pp. 3-7
Author(s):  
L.-E. Al-Badu ◽  
O. Smirnov ◽  
L. Kalachniuk
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Bile Acids ◽  
Medical Condition ◽  
Critical Role ◽  
Reproductive Function ◽  
The Body ◽  
Synthetic Analog ◽  
Taurine Deficiency ◽  
Negative Effect

Obesity is a medical condition in which excess body fat has accumulated to the extent that it may have a negative effect on health. The daily ration of an adult cat must contain 40–45% of proteins, 20–25% of fats, 25–30% of carbohydrates. Low- fat diets are recommended to cats with overweight. Necessary amino acids are in the diet of cats with excess weight. Taurine is a sulfonic acid, which synthesizes in the body of animals and humans from the amino acid of cysteine. It plays an essential role in the digestion and assimilation of fats and lipids. The need for cats in taurine is due to their limited ability to synthesize taurine from amino acids that contain sulfur, as well as the fact that it holds bile acids. The latter is very important because cats do not produce bile acid salts associated with glycine, even in the case of taurine deficiency. Taurine has many fundamental biological roles, such as conjugation of bile acids, antioxidation, osmoregulation, membrane stabilization, and modulation of calcium signaling. It is essential for cardiovascular function, and development and function of skeletal muscle, the retina, and the central nervous system. The deficiency of taurine leads to degeneration of the retina and blindness, deafness, cardiomyopathy, disorders in the functioning of the immune and reproductive systems, suppression of neonatal growth, and the occurrence of birth defects. The recommended amount for a cat per day is 100–200 mg. L-Tryptophan is an α-amino acid that is used in the biosynthesis of proteins. Together with vitamin B6, magnesium and niacin, tryptophan is responsible for the serotonin production in the brain (a mediator that regulates the activity of nerve cells and transmits signals between them). Also, tryptophan is involved in the production of hemoglobin and affects the reproductive function of animals. The recommended amount for a cat per day is 0.3 g/1000 kcal of energy value (EV). DL-methionine is a synthetic analog of natural methionine. Methionine is an essential amino acid for animals. As the substrate for other amino acids such as cysteine and taurine, and the important antioxidant glutathione, methionine plays a critical role in the metabolism and health of many species, including humans. Methionine is a source of sulfur that forms the keratin protein. Keratin is simply necessary for the health of the hair, skin, and claws of the animal. The recommended amount for a cat per day (methionine + cystine) is 1.5 g/1000 kcal EV. Nowadays the problem of overweight in small domestic animals, in particular in cats and dogs, is becoming more widespread. In order to prevent the spread of obesity, therapeutic rations should be balanced by all indicators, such as proteins, fats, carbohydrates, amino acids, minerals, and vitamins.

scholarly journals The levels of relaxin and amino acids play a critical role in women with variable degree of preparedness for labour

2021 ◽  
pp. 3-8
Author(s):  
Nikolay Shcherbina ◽  
Natalia Shelest
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Pregnant Women ◽  
Critical Role ◽  
The Body ◽  
Cervical Ripening ◽  
Birth Preparedness ◽  
Variable Degree ◽  
Functional Changes ◽  
Amino Acid Imbalance

Underlying biochemical factors that contribute towards the preparedness for labour and ripening of the cervix remain largely unknown. We aimed to characterize metabolic and hormonal determinants that constitute the preparedness for labour in women. The aim of the research was to study the content of relaxin and amino acids involved in its formation in primiparous pregnant women with various degrees of birth preparedness. Materials and methods: Prospective study has been conducted on 115 primiparous women at 38-40 weeks of gestation. Biochemical methods were used to analyse relaxin and amino acid levels in pregnant women with varying degree of birth preparedness. Results: the obtained data from the study indicate importance role of relaxin in the underlying pathogenesis in women with variable degree of preparedness for labour. The results allow to use the levels of relaxin serum as a predictor of the state of the birth canal. Furthermore, the amino acids are known to participate in various critical metabolic processes and play an important role is orchestrating many essential pathways in the body. We present the analysis of amino acids involved in the formation of relaxin in the serum of pregnant women. Our analysis has shown that amino acid imbalance leads to disruption of energy metabolism and blood flow rate, resulting in metabolic, structural and functional changes in the cervix at the onset of labour. Conclusion: considering the mechanisms of the possible influence of relaxin and amino acids on the cervical ripening, we concluded that correcting amino acid imbalance and normalising relaxin levels should be included in preinduction of labour therapeutic regimen. This would be an important step in improving the perinatal outcomes

scholarly journals Rabbit Carcasses for Use in Feline Diets: Amino Acid Concentrations in Fresh and Frozen Carcasses With and Without Gastrointestinal Tracts

2021 ◽  
Vol 7 ◽  
Author(s):  
Tammy J. Owens ◽  
Andrea J. Fascetti ◽  
C. Christopher Calvert ◽  
Jennifer A. Larsen
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Crude Protein ◽  
Protein Body ◽  
National Research Council ◽  
Body Water ◽  
Taurine Supplementation ◽  
Frozen Ground ◽  
Taurine Deficiency ◽  
Amino Acid Concentrations

Whole-prey diets for exotic feline species are common, and this practice has also increased in popularity for domestic cats. However, prior analyses of prey indicate possible essential amino acid inadequacy, and dilated cardiomyopathy from taurine deficiency was reported in cats fed whole ground rabbit. Crude protein, body water, and amino acid concentrations were evaluated in fresh and frozen ground rabbits with (n=10) or without (n = 10) gastrointestinal tracts. Amino acids were greater in fresh samples without gastrointestinal tracts (p < 0.05) except taurine, glycine, and cysteine. When normalized for protein content, only glutamate, alanine, methionine, isoleucine, tyrosine, lysine, histidine, and arginine were greater in fresh rabbits without gastrointestinal tracts (g/16 g N basis; p < 0.05). Freezing at −18°C for 30 days had no effect on crude protein or body water content. After freezing, only methionine was lower and only proline was higher when gastrointestinal tracts were omitted (g/16 g N basis; p < 0.05). Regardless, all essential amino acids except taurine exceeded Association of American Feed Control Officials and National Research Council nutrient recommendations for all feline life stages. In contrast, there was minimal impact of treatment on taurine concentrations. However, although feline taurine requirements for prey and other raw or fresh food diets remain undefined, none of the rabbit samples met any recommendation for taurine concentrations for commercial canned or dry extruded diets, ranging from 20 to 90% of the minimum values. Taurine supplementation is recommended when feeding rabbit to cats. Determination of taurine requirements of cats fed whole-prey diets is warranted.

scholarly journals Dietary supplements based on modified and enriched with amino acids zeolite in the cultivation of young turkeys

2022 ◽  
Vol 354 (11-12) ◽  
pp. 20-23
Author(s):  
S. V. Dezhatkina ◽  
N. A. Feoktistova ◽  
E. V. Pankratova ◽  
N. A. Provorova ◽  
E. S. Salmina
Keyword(s):  
Amino Acids ◽  
Hematological Parameters ◽  
Live Weight ◽  
High Growth ◽  
Mineral Elements ◽  
High Growth Rate ◽  
The Body ◽  
Control Group ◽  
Modified Zeolite ◽  
Negative Effect

Relevance. Modern turkey crosses have a genetically determined high growth rate. These farm birds are very sensitive to even minor fluctuations in their diet, are susceptible to a deficiency of amino acids, protein, mineral elements and vitamins, which can contribute to a decrease in their productivity, the development of pathological processes and diseases. The use of modern technologies and scientific achievements has made it possible to prepare a new product — modified zeolite. This natural mineral is already free of impurities and microbes, with open pore windows, has a high ability to selectively exchange, and is obtained by various methods of activating zeolite in industrial conditions. At the same time, Ulyanovsk specialists have mastered the technology of enriching modified zeolite with useful substances.Methods. The aim of the work was to study the effect on the body of turkeys and the level of their productivity of additives based on modified zeolite enriched with amino acids. The experiment was organized for 60 days on 250 turkeys of the breed Hybrid Cread-mayker aged 55–60 days in the conditions of the Ulyanovsk region. The control group received the main ration (MR), the experimental group was given once a day in addition to the MR in the morning feeding in a mixture with mixed feed 5% additives of modified zeolite enriched with amino acids.Results. The inclusion of a supplement based on modified zeolite enriched with amino acids in the diet of turkeys does not have a negative effect on the hematological parameters of their blood, all indicators corresponded to the physiological norm. During the experiment in the 2nd group, the live weight of poultry was obtained larger by 8.70%, which amounted to 12,296 kg, respectively, more profit was obtained from the sale of turkey meat, total revenue was 133,210, and additional profit was 27,960 rubles, 2.41 rubles of profit was received for 1 ruble of costs. Тhe data indicate the normalization of mineral homeostasis in the body of turkeys and better absorption of nutrients in the feed diet.

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>

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 Conversion Percentage of Tryptophan to Nicotinamide is Higher in Rice Protein Diet than in Wheat Protein Diet in Rats

2015 ◽  
Vol 8 ◽  
pp. IJTR.S22444
Author(s):  
Katsumi Shibata ◽  
Tsutomu Fukuwatari ◽  
Tomoyo Kawamura
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Body Weight Gain ◽  
Acid Value ◽  
Amino Acid Mixture ◽  
The Body ◽  
Protein Diet ◽  
Acid Mixture ◽  
Wheat Protein ◽  
Rice Protein

We reported previously that the pellagragenic property of corn protein is not only low L-tryptophan concentration but also the lower conversion percentage of L-tryptophan to nicotinamide; the amino acid composition greatly affected the conversion percentage. The amino acid value of wheat protein is lower than that of rice protein. In the present study, we compare the conversion percentages of L-tryptophan to nicotinamide between wheat protein and rice protein diets in growing rats. The body weight gain for 28 days in rats fed with a 10% amino acid mixture diet with wheat protein was lower than that of rats fed with a 10% amino acid diet with rice protein (68.1 ± 1.6 g vs 108.4 ± 1.9 g; P < 0.05). The conversion percentage of L-tryptophan to nicotinamide was also lower for the wheat protein diet compared with the rice protein diet (1.44 ± 0.036% vs 2.84 ± 0.19%; P < 0.05). The addition of limiting amino acids (L-isoleucine, L-lysine, L-tryptophan, L-methionine, L-threonine) to the wheat protein diet improved growth and the conversion percentage. In conclusion, our result supports the thinking that the composition of amino acids affects the conversion ratio of L-tryptophan to nicotinamide.

scholarly journals In vivo Determination of Amino Acid Bioavailability in Humans and Model Animals

2005 ◽  
Vol 88 (3) ◽  
pp. 923-934 ◽  
Author(s):  
Malcolm F Fuller ◽  
Daniel Tomé
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
The Body ◽  
Whole Body ◽  
Intestinal Lumen ◽  
Stable Isotope Labelling ◽  
Ileal Digestibility ◽  
Hydrolyzed Protein ◽  
Protein Free Diet

Abstract Because the digestion of many dietary proteins is incomplete, and because there is a continuous (but variable) entry into the intestinal lumen of endogenous protein and amino acid nitrogen that is also subject to digestion, the fluxes of nitrogen, amino acids, and protein in the gut exhibit a rather complicated pattern. Methods to distinguish and quantitate the endogenous and dietary components of nitrogen and amino acids in ileal chyme or feces include the use of a protein-free diet, the enzyme-hydrolyzed protein method, different levels of protein intake, multiple regression methods, and stable-isotope labelling of endogenous or exogenous amino acids. Assessment of bioavailability can be made, with varying degrees of difficulty, in man directly but, for routine evaluation of foods, the use of model animals is attractive for several reasons, the main ones being cost and time. Various animals and birds have been proposed as models for man but, in determining their suitability as a model, their physiological, enzymological, and microbiological differences must be considered. Fecal or ileal digestibility measurements, as well as apparent and true nitrogen and amino acid digestibility measurements, have very different nutritional significance and can, thus, be used for different objectives. Measurements at the ileal level are critical for determining amino acid losses of both dietary and endogenous origin, whereas measurements at the fecal level are critical in assessing whole-body nitrogen losses. A complementary and still unresolved aspect is to take into account the recycling of intestinal nitrogen and bacterial amino acids to the body.

scholarly journals The metabolic utilization of amino acids: potentials of 14CO2 breath test measurements

1992 ◽  
Vol 67 (2) ◽  
pp. 207-214 ◽  
Author(s):  
V. V. A. M. Schreurs ◽  
H. A. Boekholt ◽  
R. E. Koopmanschap ◽  
P. J. M. Weijs
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Breath Test ◽  
Relative Rate ◽  
The Body ◽  
Adult Rats ◽  
Total Oxidation ◽  
Amino Acid Utilization ◽  
Amino Acid Requirements ◽  
14Co2 Breath Test

The present paper offers a dual 14CO2 breath test approach to study the metabolic utilization of free amino acids in the body. Using the carboxyl-[14C]isotopomer of an amino acid as the test substrate the percentage recovery of the isotope as 14CO2 reflects which part of the labelled amino acid flux has been decarboxylated. The residual C fragments may flow to total oxidation at least to the level recovered for the universal [14C]isotopomer. In the case that recovery for total oxidation is less than for decarboxylation, part of the [14C]fragments are retained in the body by either exchange or non-oxidative pathways. Utilization of tyrosine and leucine was measured in the post-absorptive phase in adult rats conditioned on isoenergetic diets containing 210, 75 or 0 g protein/kg. It was shown that the level of dietary protein exerts an influence on both decarboxylation and total oxidation. Although the responses of leucine and tyrosine were not different for total oxidation, there was a difference between the amino acids in their relative rate of decarboxylation. That this dual 14CO2 breath test approach can be used as a tool to evaluate whether the protein and amino acid supply has been adequate to support actual requirements is discussed.Amino acid utilization: Amino acid requirements: Leucine: Tyrosine

scholarly journals The case for regulating indispensable amino acid metabolism: the branched-chain α-keto acid dehydrogenase kinase-knockout mouse

2006 ◽  
Vol 400 (1) ◽  
Author(s):  
Susan M. Hutson
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
Essential Amino Acids ◽  
The Body ◽  
Keto Acid ◽  
Acid Dehydrogenase ◽  
Indispensable Amino Acid ◽  
Branched Chain

BCAAs (branched-chain amino acids) are indispensable (essential) amino acids that are required for body protein synthesis. Indispensable amino acids cannot be synthesized by the body and must be acquired from the diet. The BCAA leucine provides hormone-like signals to tissues such as skeletal muscle, indicating overall nutrient sufficiency. BCAA metabolism provides an important transport system to move nitrogen throughout the body for the synthesis of dispensable (non-essential) amino acids, including the neurotransmitter glutamate in the central nervous system. BCAA metabolism is tightly regulated to maintain levels high enough to support these important functions, but at the same time excesses are prevented via stimulation of irreversible disposal pathways. It is well known from inborn errors of BCAA metabolism that dysregulation of the BCAA catabolic pathways that leads to excess BCAAs and their α-keto acid metabolites results in neural dysfunction. In this issue of Biochemical Journal, Joshi and colleagues have disrupted the murine BDK (branched-chain α-keto acid dehydrogenase kinase) gene. This enzyme serves as the brake on BCAA catabolism. The impaired growth and neurological abnormalities observed in this animal show conclusively the importance of tight regulation of indispensable amino acid metabolism.

scholarly journals Response of adult rats to deficiencies of different essential amino acids

1974 ◽  
Vol 31 (1) ◽  
pp. 47-57 ◽  
Author(s):  
A. K. Said ◽  
D. M. Hegsted ◽  
K. C. Hayes
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nutritive Value ◽  
Plasma Concentrations ◽  
Essential Amino Acids ◽  
The Body ◽  
Adult Rats ◽  
Short Period ◽  
Body Weights ◽  
Fatty Livers

1. Adult rats were fed on diets free of either lysine, methionine, threonine or protein. The threonine- and protein-deficient animals lost weight at approximately the same rate, about 100 g in 14 weeks, at which time several were moribund. In contrast, lysine-deficient animals lost only about 30 g in 14 weeks and had lost only 46 g after 22 weeks, when they were killed. Methionine-deficient animals showed an intermediate response. Losses in weight of several tissues – kidney, heart and two muscles – were related to, but not necessarily proportional to, the loss of body-weight. Liver weights relative to body-weights were large in lysine- and threonine-deficient animals and smallest in methionine-deficient animals.2. Adult rats were fed on diets containing zero, a moderate amount (about twice the estimated minimal requirement) or an excess (about four times the estimated requirement) of lysine or threonine in all combinations (3 × 3 design). Analysis of variance of the body-weights, tissue weights and tissue nitrogen contents indicated, in general, a significant effect of each amino acid, as expected, but also, in most instances, a significant interaction. Plasma concentrations of lysine and threonine were affected by the intakes of the respective amino acids, but plasma lysine concentrations were also affected by the threonine intake.3. Liver histology also suggested significant interactions between the two amino acids. Animals given no lysine but moderate amounts of threonine developed severely fatty livers; next most severely affected were animals receiving excess of both amino acids. Threonine deficiency, in the presence or absence of lysine, produced moderately fatty livers similar to those seen in protein-deficient animals.4. Since animals have varying ability to conserve body nitrogen when they are fed on diets limiting in different essential amino acids, measurements of biological value (BV) and net protein utilization by conventional methods, over a short period of time, over-estimate nutritive value relative to amino acid score and probably over-estimate the true nutritive value of poor-quality proteins, particularly those limiting in lysine. If so, this is a serious error, since it leads to underestimates of the protein requirements if BV is used. The fact that certain tissues, particularly the liver, do not necessarily lose nitrogen in proportion to total body nitrogen and may show specific pathological effects depending on the limiting amino acid or the proportions of amino acids in the diet also indicates that general measures of nitrogen economy may not be sufficiently discriminating tests of the nutritive value of proteins.

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