scholarly journals Adsorption of protein breakdown products and toxins by erythrocytes

2020 ◽  
Vol 22 (2) ◽  
pp. 239
Author(s):  
Z. Blyumshteyn

It has been established that amino acids enter the bloodstream through the intestinal walls in an unchanged form, and both these substances and parenterally administered protein breakdown products cannot be detected either in serum or in whole blood soon after their introduction. BI Zbarsky (Zhurn. Exp. Biol., 1925, No. 1) explains this fact by the adsorption of protein breakdown products by blood erythrocytes, from which these products can be easily separated by simple boiling, and which transfer these products to the cells of the body.

1983 ◽  
Vol 64 (3) ◽  
pp. 315-320 ◽  
Author(s):  
F. J. Ballard ◽  
J. L. Burgoyne ◽  
F. M. Tomas ◽  
J. L. Penfold

1. Creatinine and Nτ-methylhistidine excretion rates have been measured in 13 hypopituitary children to calculate the body muscle contents and rates of myofibrillar protein breakdown. Analyses have been made during periods of growth hormone withdrawal and subsequent administration. 2. The creatinine excretion rate was lower in the hypopituitary children, indicating a lower muscle content per kg body weight. This difference persisted even in children who had received growth hormone for several years. 3. Excretion of Nτ-methylhistidine was reduced by the administration of growth hormone. 4. The fractional breakdown rate of myofibrillar protein, as calculated from the Nτ-methylhistidine to creatinine molar excretion ratio, averaged 1.76%/day in the four youngest children during growth hormone withdrawal. This was significantly higher than for control children of a similar age (P < 0.02) and was reduced to the normal rate of 1.47%/day by growth hormone administration. 5. in older children the fractional rate of myofibrillar protein degradation remained in the normal range irrespective of growth hormone treatment. 6. These results are discussed in the context of the anabolic effects of growth hormone on muscle being partly explained by its action to decrease rates of protein breakdown.


2004 ◽  
Vol 17 (1) ◽  
pp. 77-88 ◽  
Author(s):  
Thomas C. Vary ◽  
Christopher J. Lynch

Sepsis initiates a unique series of modifications in the homeostasis of N metabolism and profoundly alters the integration of inter-organ cooperatively in the overall N and energy economy of the host. The net effect of these alterations is an overall N catabolic state, which seriously compromises recovery and is semi-refractory to treatment with current therapies. These alterations lead to a functional redistribution of N (amino acids and proteins) and substrate metabolism among injured tissues and major body organs. The redistribution of amino acids and proteins results in a quantitative reordering of the usual pathways of C and N flow within and among regions of the body with a resultant depletion of the required substrates and cofactors in important organs. The metabolic response to sepsis is a highly integrated, complex series of reactions. To understand the regulation of the response to sepsis, a comprehensive, integrated analysis of the fundamental physiological relationships of key metabolic pathways and mechanisms in sepsis is essential. The catabolism of skeletal muscles, which is manifested by an increase in protein degradation and a decrease in synthesis, persists despite state-of-the-art nutritional care. Much effort has focused on the modulation of the overall amount of nutrients given to septic patients in a hope to improve efficiencies in utilisation and N economies, rather than the support of specific end-organ targets. The present review examines current understanding of the processes affected by sepsis and testable means to circumvent the sepsis-induced defects in protein synthesis in skeletal muscle through increasing provision of amino acids (leucine, glutamine, or arginine) that in turn act as nutrient signals to regulate a number of cellular processes.


2020 ◽  
Vol 11 (SPL4) ◽  
pp. 2756-2767
Author(s):  
Vijaya Vemani ◽  
Mounika P ◽  
Poulami Das ◽  
Anand Kumar Tengli

In the preservation of normal physiological functions, the building blocks of the body called amino acids play a crucial role. A number of valuable and nutritional phytoconstituents are contained in fruit juices, such as vitamins, minerals, microelements, organic acids, antioxidants, flavonoids, amino acids and other components. Due to the growing population and demand, the quality of fruit juices is decreasing. One of the unethical and harmful practices called adulteration or food fraudulence has been adopted by most food and beverage industries. The amino acids which is one of the most important phytochemicals of fruit and fruit juices which affects the organoleptic properties like color, odor, and taste of juices and also helps in authenticity process from governing bodies by providing total amino acid content. Consequently, the main aim of the present review work is to provide information regarding the importance of amino acids, how they are adulterated, the potential analytical approach to detected amino acids and which methods are generally accepted method by the food industries. According to the literature review, we presume that reverse phased high-performance liquid chromatography with pre-column derivatization was the most adopted method for quality checking due to its advantages over other old and recent analytical approaches like simple, rapid, cost-effective nature, less / no sample matrix effect with high sensitivity, accuracy, and precision.


2017 ◽  
Vol 9 (2) ◽  
pp. 98 ◽  
Author(s):  
Afifa Khalida ◽  
Agustono Agustono ◽  
Widya Paramita

                                                                   AbstrakAsam amino adalah komponen terkecil yang menyusun protein. Sejumlah asam amino akan dihubungkan satu sama lain melalui perantara ikatan peptida untuk membentuk protein. Asam amino telah dibagi menjadi dua; yaitu asam amino esensial dan asam amino non-esensial. Asam amino esensial adalah asam amino yang tidak dapat disintesis oleh tubuh ikan; karena itu asam amino esensial harus ada dalam pakan. Lisin adalah salah satu dari sepuluh asam amino esensial, fungsi lisin adalah untuk pertumbuhan dan perbaikan jaringan tubuh. Penelitian ini bertujuan untuk mengetahui pengaruh lisin dalam pakan komersial terhadap retensi protein dan retensi energi ikan bawal air tawar. Metode yang digunakan adalah desain eksperimen rancangan acak lengkap. Perlakuan yang digunakan adalah kadar lisin yang berbeda, yaitu P0 (0%), P1 (0,6%), P2 (1,2%), P3 (2,4%), P4 (4,8%) dan perlakuan  diulang 4 kali. Parameter utama yang diamati adalah retensi protein dan retensi energi pada air tawar bawal. Parameter yang diukur didukung oleh parameter kualitas air. Analisis data menggunakan Analisis Varian (ANOVA) dan untuk menentukan perlakuan terbaik digunakan Duncan's multiple range test. Hasil penelitian menunjukkan perbedaan yang signifikan (p <0,05) dalam retensi protein dan energi adalah daging ikan bawal air tawar. Retensi protein dan retensi energi dalam pengobatan P1 (0,6% lisin), P2 (1,2% lisin), P3 (2,4% lisin) dan P4 (4,8% lisin) berbeda secara signifikan dengan perlakuan P0 (kontrol). Kualitas air selama 40 hari perlakuan ditetapkan pada suhu 27-300 C, pH 7,5-8,5, amonia 4 mg / l dan oksigen terlarut 4 mg / l.                                                                 AbstractAmino acids are the smallest components that compose proteins. A number of amino acids will be conducted to one another through the intermediary of peptide bonds to form proteins. Amino acids have divided into two; those are essential amino acids and non-essential amino acids. The essential amino acids are amino acids that can not be synthesized by the body of fish; therefore the essential amino acids must be in feed. Lysine is one of the ten essentials amino acids , the function of lysine are for the growth and repair body tissues. This research was aimed to determine the effect of lysine in commercial feed on protein retention and energy retention of freshwater Bawal.The method used is experiment with a completely randomized design as an experimental design. The treatment used is different lysine levels , namely P0 ( 0 % ) , P1 ( 0.6 % ) , P2 ( 1.2 % ) , P3 ( 2.4 % ) , P4 (4.8 % ) and treatment was repeated 4 times. The main parameters were observed protein retention and energy retention on Bawal fresh water. Parameters measured were supported by water quality parameters. Analysis of the data using Analysis of Varian ( ANOVA ) and to determine the best treatment used Duncan 's multiple range test. The results showed the significant differences ( p < 0.05 ) in protein retention and energy were freshwater pomfret fish meat. Retention of protein and energy retention in treatment P1 ( 0.6 % lysine ) , P2 ( 1.2 % lysine ) , P3 ( 2.4 % lysine ) and P4 ( 4.8 % lysine ) was significantly different with treatment P0 ( control ). The quality of water for 40 days treatment was set to temperature 27-300 C, pH 7.5-8.5, ammonia 4 mg/l and dissolved oxygen 4 mg/l.


2020 ◽  
Vol 11 (4) ◽  
pp. 403-417
Author(s):  
Gr. N. Egorov

The abdominal cavity is, in essence, an appendage of the lymphatic system, therefore, it cannot represent a completely foreign container for the blood poured out here. Indeed, the observations of Virchow, Wintrich and others show that whole blood can remain in this cavity for a long time (several days) without undergoing clotting (Pashutin). In view of this fact, it is natural to expect, as is confirmed by experiments, that most of the blood that has entered the abdominal cavity has time to be absorbed before it begins to coagulate. If a part of it, which failed to be absorbed in time, undergoes clotting, then this does not represent any particular disturbances in the overall economy of blood, the blood clot is completely absorbed after preliminary disintegration (fat). In this sense, hemorrhage into the abdominal cavity is not life-threatening, since the blood does not disappear for the body, but soon again, almost entirely, enters the total mass of the blood vessel.


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

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.


2021 ◽  
Author(s):  
Bharti Koshti ◽  
Ramesh Singh ◽  
Vivekshinh Kshtriya ◽  
Shanka Walia ◽  
Dhiraj Bhatia ◽  
...  

<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>


1957 ◽  
Vol 1957 ◽  
pp. 3-15 ◽  
Author(s):  
D. G. Armstrong ◽  
K. L. Blaxter ◽  
N. McC. Graham

The work of the late Sir Joseph Barcroft and his collaborators (see Elsden & Phillipson, 1948) left little doubt that, in ruminants, the end products of the bacterial dissimilation of dietary carbohydrate included large amounts of the steam-volatile fatty acids—acetic, propionic and butyric acids. More recently, el Shazly (1952a, b) has shown that the steam-volatile fatty acids also arise together with ammonia during the bacterial breakdown of amino-acids in the rumen. Studies by Pfander & Phillipson (1953) and Schambye (1955) further indicate that the acids are absorbed from the digestive tract in amounts that suggest they make a major contribution to the energy requirement of the animal. Quantitative data relative to the amounts absorbed, however, are difficult to obtain. Carroll & Hungate (1954) have calculated that in cattle some 6,000-12,000 Cal. of energy are available from the acids produced by fermentation in the rumen. With sheep, Phillipson & Cuthbertson (1956) have calculated from the results of Schambye (1951a, b; 1955) that at least 600-1,200 Cal. of energy in the form of steam-volatile fatty acids could be absorbed every 24 hrs. Since the fasting heat production of the steer is about 6,500 Cal./24 hrs. and that of the sheep about 1,100 Cal./24 hrs. it is clear that if the fatty acids can be utilised efficiently by the body tissues, they could make a major contribution to the energy requirements, at least those for maintenance.


Author(s):  
Alan Kelly

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!


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