Oligosaccharida
Monosaccharides
- glucose
- fructose
- galactose
- mannose
- Disaccharides
- sakharoza (ordinary sugar)
- maltose
- isomaltosis
- lactose
- lactulose
- dextrin
- glycogen
- starch
- cellulose
Proteins - The main "workers" cells are natural biopolymers built from residues 20 amino acids. The macromolecule proteins can be part of several tens to hundreds of thousands and even millions of amino acid residues, and the protein properties are significantly dependent on the order in which these residues are located for each other. For this reason, it is obvious that the number of possible proteins is practically unlimited.
Amino acids Call organic compounds in which the carboxyl (acid) group of the Soon and the amino group NH 2. Attached to the same carbon atom.
Fig.1 Structural formula amino acids
The structure of such a molecule is described by the structural formula (Fig. 1), where R is a radical, different for different amino acids. Τᴀᴋᴎᴍ ᴏϭᴩᴀᴈᴏᴍ, the composition of amino acids include four organogen C, O, N, N, and some radicals can be included in S.
According to the ability of a person to synthesize amino acids from their predecessors, they are divided into two groups:
- Indispensable: tryptophan, phenylalanine, lysine, threonine, methionine, leucine, isoleucine, Valin, Arginine, Gistidin;
- Replaceable: tyrosine, cysteine, glycine, alanine, serine, glutamy acid glutamine, asparagic acid, asparagin, proline
An indispensable amino acids should flow into the human body with food, as they are not synthesized by a person, although some replaceable amino acids are synthesized in the human body in insufficient quantities and should also come with food.
Chemical formulas 20 standard amino acids:
The structure of a protein molecule supported by covalent bonds between amino acid residues is called primary.In other words, the primary structure of the protein is determined by the simple sequence of amino acid residues. These remnants can be quite defined in space, forming secondarystructure. The most characteristic secondary structure is the α-helix when the amino acid chains seem to form the screw threads. One of the most amazing properties of the macromolecule is that the α-spirals with the left and right "threads" are in nature with a substantially different probability: macromolecules, "swirling" to the right, almost no.The asymmetry of biological substances relative to the mirror reflection found in 1848 ᴦ. Great French scientist L. Paster. Subsequently, it turned out that this asymmetry is inherent in not only macromolecules (proteins, nucleic acids), but also organisms in general. As the preferential spirality of the macromolecules arose and how she further fixed in the course of biological evolution - these questions are still discussion and have no one-time response.
The most complex and delicate features of the structure that distinguish one protein from the other are associated with a spatial organization of a protein called tertiarystructure. In fact, it is about the fact that the spiral chains of amino acid residues are minimized into something resembling a ball of thread; As a result, rather long chains occupy a relatively small volume in space. The collapse character in the ball is not accidental. On the contrary, it is definitely determined for each protein. It is due to the tertiary structure of a protein that is capable of performing its unique catalytic, enzymatic functions, when, as a result of the fastened capturing of the reagents, their synthesis is carried out in complex chemical comparable, comparable in difficulties with the protein itself. None of the chemical reactions carried by proteins cannot occur in the usual way.
In addition to the tertiary structure, the protein may have quaternarystructure; When there is a structural connection between two or several proteins. In fact, it is about combining several "clubs" from polypeptide chains.
Nucleic acids (from lat. nucleus. - core) - high molecular weight organic phosphorus-containing combined, biopolymers. Polymer forms of nucleic acids call polynucleotides. The chains from nucleotides are connected through the residue of phosphoric acid (phosphodieter communication). Since in nucleotides there are only two types of heterocyclic molecules, ribosis and deoxyribosis, then there are only two types of nucleic acids - deoxyribonucleic ( DNA) and ribonuclear ( RNA). DNA and RNA nucleic acids are present in the cells of all living organisms and perform the most important functions for storing, transferring and implementing hereditary information. One of the basic axes of biology claims that hereditary information on the structure and functions of the biological object is transmitted from generation to generation by the matrix path, and the carriers of this information are nucleic acids.
These biopolymers are easier at first glance than proteins. The "alphabet" of nucleic acids consists of two of the four "letters", in the role of which nucleotides are speaking - sugar-pentoses, to which one of five nitrogenous grounds are attached: guanine (g), adenine (a), cytosine (C) , Timin (t) and uracil (y).
 | |||
| Adenin | Guanian | Timin | Cytozin |
Fig.2 of the foundations of the bases most common in the DNA
In ribonucleic acid (RNA), sugar is a ribosis carbohydrate (C 5 H 10 O 5), and in deoxyribonucleic acid (DNA) - carbohydrate deoxyribosis (C 5 H 10 O 4), which differs from ribose only by the fact that about one of the atoms Carbon The group is replaced by a hydrogen atom. Three of these nitrogen bases - G, A and C - are included in the composition and RNA, and DNA. The fourth nitrogenous base in these acids is different - t applies only to DNA, and only in RNA. The links of nucleotides with phosphodieter bonds of phosphoric acid residue H 3 PO 4 are associated. Relative molecular weights of nucleic acids reach the values \u200b\u200bof 1500,000-2,000,000 or more. The secondary structure of DNA was established by X-ray analysis methods in 1953 ᴦ. R. Franklin, M. Wilkins, J. Watson and F. Scream. It turned out that the DNA form spirally twisted threads, and the nitrogen base of one DNA filament is associated with hydrogen bonds with a determined base of another thread: adenine can only be associated with thimine, and cytosin is only with guanin (Fig. 3). Such connections are called complementary(Additional). Hence it follows that the order of the base in one thread uniquely determines the order in another thread. It is with this that the most important DNA property is connected - the ability to self-reproduction (replication). RNA has no double spiral structure and is built as one of the DNA threads. There are ribosomal (RRNA), matrix (mRNA) and transport (TRNA). ʜᴎʜᴎ are distinguished by those roles that play cells.
Fig. 3 Different DNA DNA Spirals
What do nucleotide sequences in nucleic acids mean? Every three nucleotides (they are called triplet or codons)encode a particular amino acid in protein. For example, the UCG sequence gives a signal to the synthesis of amino acid serine. Immediately the question arises: how many different triples can be obtained from four "letters"? It is easy to figure out that such triples can be 4 3 \u003d 64. But in the formation of proteins, 20 amino acid residues can participate, it means some of them can be encoded by different three, which is observed in nature. For example, leucine, serine, arginine is encoded with six top three, proline, valine and glycine - four, etc. This property of a triplet genetic code is customary degenerate or redundancy.It should also be noted that for all living organisms, protein coding occurs equally (coding versatility). At the same time, the sequences of nucleotides in DNA are not read differently, as the only way (Non-induction of codons).
Xylose (wood sugar) is contained in a cotton husk, corn noras. Xylose is part of Penosanov. Connecting with phosphorus, xylose proceeds to active compounds that play an important role in the mutual adventures of sugars. Arabinose is contained in coniferous ... [Read more]
The patterns of formation and accumulation of polysaccharides in plants. The role in the life of polysaccharides plants is 80% of the organic matter of the planet, since they make up most of the dry matter of the plants. In the plants of monosaccharides and their derivatives, ... [Read more]
The main reserve polysaccharide in plant cells is starch. Starch is formed in plants with photosynthesis and postponed in the form of a "reserve" carbohydrate in roots, tubers and seeds. For example, rice grains, wheat, rye and other cereals contain 60-80% starch, ...
What amino acid aromatic
B) Asparagic acid
C) cysteine
D) tryptophan +
E) GISTIDIN
109. What amino acid heterocyclic:
A) GISTIDIN +
What amino acid is manifested
B) Asparagic acid
D) phenylalanine
111. Specify the dustyrion of amino acids:
B) 
C) 
D) 
+
E) 
112. What is the peptide connection:
A) 
113. Amino acid, in the molecule of which there is no asymmetric carbon atom:
A) Tyrosine
C) glycine +
D) phenylalanine
In the composition of which amino acid is sulfur
A) Arginine
B) tryptophan
C) GISTIDIN
D) cysteine \u200b\u200b+
115. Amino acid, in which there is no free amino group in the molecule:
A) Proline +
B) cysteine
C) glutamic acid
D) tryptophan
E) phenylalanine
116. If the pH of the amino acid solution is equal to the value of the isoelectric point, then:
A) Amino acid molecule charged negatively
B) amino acid molecule charged positively
C) Amino acid molecule neutral +
D) amino acid soluble in water
E) amino acid molecule easily collapsed
117. If the pH of the amino acid solution is equal to the value of the isoelectric point, then:
A) Amino acid molecule in the form of bipolar ion +
B) anion amino acid molecule
C) molecule amino acids in the form of cation
D) amino acid molecule is not charged
E) amino acid molecule collapses
118. In the composition of the protein molecule does not occur:
A) Creatine phosphate +
B) glutamine
D) Gistidin
E) tyrosine
119. glycine \u003d 2.4, RK2 glycine \u003d 9.7, the isoelectric point of glycine is equal to:
120. The protein molecule includes:
A) carboxylic acid
B) D--amino acids
C) D--amino acids
D) l--amino acids
E) L--amino acids +
121. Amino acid, which does not occur in the composition of the protein molecule:
A) tryptophan
B) Asparagic acid
D) Ornithine +
E) GISTIDIN
122. It does not apply to replacement amino acids:
C) glutamic acid
D) tryptophan +
123. Not applicable to indispensable amino acids:
B) phenylalanine
D) proline +
E) threonine
124. Replaced amino acids include:
B) Isoleucine
C) Asparagic acid +
D) methionine
E) tryptophan
125. An indispensable amino acids include:
B) glutamic acid
D) Asparagin
E) cysteine
126. Ningidrin reaction - high-quality response to:
A) free amino groups +
B) free carboxyl groups
C) to determine hydroxyl groups
D) to define sh-groups
E) to determine aromatic amino acids
127. To determine the protein in the solution, use:
A) Selivanov Reaction
B) Biuret reaction +
C) Sakaguchi Reaction
D) nitroprusside reaction
E) Millon Reaction
128. Millon Reaction is used: to determine:
A) tyrosine residues in the protein molecule +
B) Guanidine Arginine Group
C) hytidine imidazole group
D) aromatic amino acids
E) cysteine \u200b\u200bSH
129. What amino acid dicarboat:
A) Tyrosine
B) glutamic acid +
D) tryptophan
130. As part of the hemoglobin molecule:
A) 1 subunit
B) 3 subunits
C) 6 subunits
D) 4 subunits +
E) 2 subunits
131. How many subunits in the albumin molecule are:
132. If the pH of the protein solution is higher than the value of the isoelectric point of the protein molecule, then:
A) protein molecule charged negative +
B) protein molecule charged positively
C) protein molecule is uncharged
D) protein molecule denaturized
E) insoluble protein
133. Not applicable to globular proteins:
A) Tripsin
B) hemoglobin
C) keratin +
D) albumin
E) Mioglobin
134. It does not apply to fibrillar proteins:
A) Collagen
B) insulin +
C) keratin
E) Elastin
135. Glycoprotein includes:
A) Phosphants
B) Carbohydrates +
E) Metal ions
136. Protein molecule in isoelectric point:
A) charged negative
B) charged positively
C) Common charge is zero +
D) denaturized
E) soluble in solution
137. For enzymatic activation, amino acids are required:
138. The composition of hemoglobin includes:
A) Marganese
B) Molybdenum
E) Iron +
139. The Prosthetic group of Mioglobin is:
B) Molybdenum
C) magnesium ions
D) copper ions
E) thiaminepyrophosphate
140. In the formation of the tertiary structure of the protein molecule, communications are involved:
A) covalent bonds
B) hydrogen bonds
C) hydrophobic interactions
D) ion interactions
E) all of the indicated links +
141. The protein that has a quaternary structure:
A) hemoglobin +
B) Ribonuclease.
C) Albumin
D) Mioglobin
E) Insulin
142. Molecular oxygen carrier in the body:
A) Amilaza
B) Albumin
C) hemoglobin +
E) Collagen
143. The composition of phosphoproproteins includes:
B) phosphates +
C) Carbohydrates
E) Metal ions
144. The protective function in the body is performed:
A) immunoglobulins +
B) Albumin
C) Histons
D) phosphatase
145. The function that proteins are performed in the body:
A) Transport
B) Protective
C) Regulatory
D) structural
E) all specified functions +
146. Lipoprotein is a protein containing in its composition:
B) Metal ions
C) Carbohydrates
D) lipids +
E) phosphates
147. Nucleoproteins are:
A) complex proteins that include lipids
B) Nucleic acid complexes with proteins +
C) complex proteins that include carbohydrates
D) complex proteins that include phosphates
E) complex proteins that include metal ions
148. For pepsin activity:
A) the pH of the medium should be equal to pH 1.5-3.0 +
B) Wednesday must be neutral
C) Wednesday must be alkaline
D) Metal ions should be present in the environment
E) There must be free amino acids in the environment
149. Blood protein, binding fatty acids:
A) hemoglobin
B) albumin +
C) Orosemicoid
D) Gaptoglobin
E) Immunoglobulin
150. In the process of reaminting, amino acids are formed:
A) -Basic acids +
B) Aldehydes
D) unsaturated hydrocarbons
E) Oxycycles
151. The buffer properties of amino acids are due to:
A) the presence of a carboxyl group
B) the presence of an amino group
C) good solubility
D) the character of the radical
E) the presence in the molecule at the same time carboxyl and amino groups +
152. Tyrosine is formed in the liver from:
A) tryptophana
B) phenylalanine +
D) histidine
E) Arginine
153. Amino acids are used in the body:
A) for protein synthesis
B) for hormone synthesis
C) for formations
D) as a source of nitrogen for the synthesis of nitrogenous compounds of non-synthesis
E) in all indicated cases +
154. In the urea cycle, it is formed:
B) Isoleucine
C) GISTIDIN
D) arginine +
E) tryptophan
155. In the body enzymes:
A) catalyze the speed of the chemical reaction +
B) perform a structural function
C) Spare Fund of Chemical Energy for Anabolic Reactions
D) perform a protective function
E) regulate osmotic pressure
156. Redox reactions catalyze:
A) oxidoreductase +
C) Hydrolase
D) Transferase
157. Enzymes catalyzing the transfer of atoms and atomic groups:
B) transferase +
C) oxidoreduktase
D) hydrolase
158. Enzymes catalyzing hydrolysis of chemical ties:
A) oxidoreductase
B) Transferase
D) hydrolase +
159. Enzymes, catalyzing isomerization reactions:
A) oxidoreductase
B) Transferase
C) isomerase +
D) hydrolase
160. Enzymes catalyzing new communication education reactions:
A) Ligases +
B) hydrolase
C) Transferase
D) Isomerase
E) oxidoreduktase
161. Enzymes, catalyzing reactions of nonregrolitic splitting and dual communication formation:
A) Hydrolase
B) Transferase
C) Isomerase
D) oxidoreduktase
162. The class of hydrolazes belongs:
A) Esterase
B) Proteinase
C) glycosidase
E) all of the specified enzyme classes +
163. Oxidoreduktases do not include:
A) lactate dehydrogenase
B) AlcoholDehydrogenase
C) Peroxidase
D) cytochromoxidase
E) Ribonuclease +
164. Apochanim is:
A) Prostum group
B) protein associated with a prosthetic group +
C) the protein part of the enzyme, the active form of which contains a coenzyme
D) organic enzyme cofactors
E) simple protein
165. Nicotinamedadenindinucleotide - a coenzyme that transfers:
A) Metyl groups
B) alkyl groups
C) acyl groups
D) amine groups
E) hydrogen atoms +
166. It does not apply to the coecments:
A) Flavinmonucleotide
B) pyridoxalphosphate
C) thyroxin +
D) nicotinamidadenindinucleotide
E) thiaminepyrophosphate
167. The coenzyme that carries the acyl groups:
A) nicotinamidadenindinucleotide
B) pyridoxalphosphate
C) Flavinmonucleotide
D) coenzyme a +
E) folic acid
168. It does not apply to the properties of enzymes:
A) does not reduce the energy of the activation of chemical reactions +
B) action efficiency
C) high specificity in relation to the substrate
D) reduces chemical reaction activation energy
E) specificity of the action relative to the type of chemical reaction
169. Hydrolysis of esters catalyzed:
A) Esterase +
B) glycosidase
C) Hydrolase
D) proteinase
E) synthetases
170. The coenzymes include:
A) Tetrahydrofolytic acid
B) thiaminepirophosphate
C) Flavyenyenindinucleotide
D) Liipoamid.
E) all specified compounds +
171. Does not apply to proteolytic enzymes:
A) Tripsin
B) lipase +
D) Elastasa
E) chymotrypsin
172. Proteolytic enzymes catalyze:
A) hydrolysis of peptide communication +
B) hydrolysis of glycoside
C) hydrolysis of ester communication
D) phosphoether hydrolysis
E) Simple Ether Communication Hydrolysis
173. Enzymes are:
A) biological catalysts accelerating chemical reactions +
B) Main Building Material of Cell Membranes
C) substances providing the detoxification of the body
D) Chemical Reaction Inhibitors
E) Substances participating in the transmission of signaling information
174. Competitive inhibitors:
A) associated with substrates
B) associated with the active center of the enzyme +
C) do not bind to the enzyme-substrate complex
D) do not bind to the active center of the enzyme, are associated with another segment of the enzyme
E) associated with the alto-solid center of the enzyme irreversibly
175. Non-competitive inhibitors:
A) like its structure substrate
B) differ in their structure from the substrate +
C) associated with the active center of the enzyme
D) denaturing enzyme
E) associated with the substrate
176. Protein enzyme Pepsin:
A) functions in gastric juice at pH 1.5-3.0 +
B) operates in gastric juice at pH 9.0-11.0
C) is included in the intestinal mucosa
D) functions in a small intestine
E) Provides hydrolysis of triacylglycerides in adipose tissue
177. Tripsin is synthesized as a predecessor in:
B) pancreas +
C) fine intestines
D) adipose tissue
E) Gastric mucosa
178. The activity of enzymes is associated with:
A) Wednesday temperature
B) pH environment
C) presence in the environment of various chemical compounds
D) substrate nature
E) with all the specified conditions +
179. Enzymes accelerate the flow of chemical reactions, as:
A) reduce the activation energy of the chemical reaction +
B) increase the activation energy of the reaction
C) reduce the concentration of the reaction product
D) change the structure of the substrate
E) change the concentration of starting materials
180. The nucleotide does not include:
A) the residue of phosphoric acid
B) pyrimidine bases
C) Purine doping
D) deoxyribosis
E) glucose +
181. The composition of ribonucleosides includes:
B) nitrogenous base and rombing +
E) the residue of phosphoric acid and rombosis
182. The DNA does not include:
B) Uracil +
E) cytosin
183. The RNA includes:
A) 2-D-deoxyribofyranosis
B) Glucopian
C) d-ribofuranosis +
D) fruitfuranoza
E) Arabinose
184. Nucleotide is:
A) adenosine
C) adenilic acid +
E) cytosin
185. The composition of deoxyribonucleotides includes:
A) the residue of phosphoric acid and a nitrogen base
B) nitrogenous base and rombosis
C) nitrogenous base and deoxyribosis
D) the residue of phosphoric acid and deoxyribosis
E) the residue of phosphoric acid, deoxyribosis and a nitrogen base +
186. A nitrogen base that is not included in RNA:
E) cytosin
187. The DNA contains:
A) Galactopianosa
B) Glucopian
C) d-ribofuranosis
D) fruitfuranoza
E) 2-D-deoxyribofyranosis +
188. Nucleoside is not:
A) Guanozin
B) Riboso-5-phosphate +
C) adenosine
E) citidine
189. Monomeric units of nucleic acids are:
A) nucleotides +
B) nitrogenous bases
C) amino acids
D) Ribosophosphate
E) monosaccharides
190. In nucleic acid molecules, nucleotides are associated:
A) disulfide bonds
Sulfur - element VI of a group of periodic system with atomic number 16. The sulfur is relatively resistant in a free state, under normal conditions is in the form of an S8 molecule having a cyclic structure. The natural sulfur consists of a mixture of four stable isotopes with AT. m. 32, 33, 34 and 36. In the formation of chemical bonds of sulfur, all six electrons of the external electron shell may use (sulfur degrees: 0, 2, 4 and 6).
The sulfur is a crystalline (in the form of a dense mass) or amorphous shape (fine powder). According to its chemical properties, sulfur is a typical metalloid and combined with many metals.
In nature, sulfur occurs both in native state and in the composition of sulfur and sulfur minerals (gypsum, sulfur coledan, Glauberova salt, lead shine, etc.).
The Russian name of the element comes from the ancient Indian (Sanskrit) the words "Sira" - light yellow. Prefix "Tio", often applied to sulfur compounds, is derived from the Greek name of the sulfur - "Teion" (Divine, Heavenly), since sulfur has long been a flammability symbol; The fire was considered the property of gods while Prometheus, as the myth says, did not bring him to people.
Seres is famous for humanity from ancient times. Meeting in nature in a free state, she paid attention to the characteristic yellow color, as well as the sharp smell that her burning was accompanied. It was also believed that the smell and blue flame propagating burning gray, distinguishes demons.
Sulfurous anhydride - suffocating gas formed when burning sulfur, in antiquity used for whitening tissues. When excavations, Pompeii found a picture on which the baking sheet with a gray and a device for hanging the matter above it. Frequently used sulfur and its compounds for the preparation of cosmetics and for the treatment of skin diseases. And for a long time it began to use it for military purposes. So, in 670, Constantinople defenders burned the Arabic fleet with the help of "Greek fire". It was a mixture of nitrate, coal and sulfur. The same substances were part of the black powder, used in Europe in the Middle Ages and until the end of the XIX century.
In hydrogen and oxygen compounds, sulfur is in the composition of various anions, forms many acids and salts. Most sulfur-containing salts are smallly soluble in water.
Sulfur forms oxygen oxides, the most important of which are sulfur and sulfuric anhydrides. Being in one group with oxygen, sulfur has similar redox properties. With sulfur hydrogen forms gas-soluble gas - hydrogen sulfide. This gas is very toxic, due to its ability to firmly bind to copper cations in the enzymes of the respiratory chain.
Sulfuric acid, one of the most important sulfur compounds was opened, apparently, to the X B, starting from the XVIII century, it is produced on an industrial scale and soon it becomes an essential chemical product, necessary in metallurgy, and in the textile industry, and in other, various industries. In this regard, even more intensive searches of the sulfur deposits began, studying the chemical properties of the sulfur and its compounds and the improvement of methods for extracting them from natural raw materials.
Introduction ....................................................................................................................... ..
Nutrition assessment ................................................................................. ..
Sulfur………………………………………………………………………………………………………
Amino acids protein ................................................................................................
Enrichment of rations of gray ...................................................................................
The influence of sulfur on the curves of animals ............................................................ ..
Introduction
The creation of a solid feed base is not only an increase in production and improving the quality of feed of different species, but first of all the introduction of highly efficient methods and means of their production, preparations that promote high digestibility of animal nutrients contained in feed and ensuring their rational use.
Feeding affects the development, growth intensity, body weight and animal reproductive functions. Only with full recruitment and birds with high-quality feeds can be successfully developing animal husbandry. Of all environmental factors, feeding has the greatest impact on productivity. In the structure of the cost of animal products, the proportion of feed is in the production of milk 50-55%, beef - 65-70%, pork - 70-75%.
In modern animal husbandry, much attention is paid to ensuring balanced nutrition of animals. Applying scientifically based feeding systems, it is possible to increase the productivity of animals and effectively use feed. In the process of nutrition, composite substances affect the animal organism are not isolated from each other, but in the complex. The balance of the components of the feed in accordance with the needs of animals is the main indicator of this complex.
Nutrition assessment
For animal husbandry, not only quantity, but mainly the quality of the feed, i.e. Their value is determined by the content of nutrients. Supported with such diet and feed, which contain all the animal substances necessary for the body and are capable of providing normal administrations of all its physiological functions for a long time.
Under the nutritionality understand the property of the feed to satisfy the natural needs of animals in food. It is possible to determine the feed nutritionally only in the process of its interaction with the organism in the physiological state of the animal and the change in its productivity. The feed nutrition cannot be expressed by any one indicator. Studies conducted by scientists of the role of individual nutrients in the life of the animal organism allowed us to conclude the need for a comprehensive nutritional evaluation system. This assessment is made up of the following data: the chemical composition of the feed and its calorieness; digestibility of nutrients; total (energy) nutrition; protein, mineral and vitamin nutrition.
To estimate feed nutrition, their chemical composition and basic processes occurring in the conversion of feed nutrients in animal husbandry products are necessary. The method of estimating feed nutritional feeds on digestible nutrients has its drawbacks, since the digestion of feed is the assimilation of only parts of the nutrients of the animal feed and the first metabolism of the metabolism between the organism and the medium. Not all digested nutrients are equally used by the body for the livelihoods and formation of products. For example: Wheat bran and barley grain have almost the same amount of nutrients (60-62%), but the productive action of bran is about 25% lower than barley. In addition, one part considered digestible is in fact destroyed by microorganisms to form carbon dioxide, methane and organic acids, the other part is derived from the body with liquids in the form of urea and heat. Thus, for a more complete assessment of feed nutrition and rations, it is necessary to know the final feedback results, i.e. What part of the digestible nutrients of each feed is absorbed by the body and turns into part of the body of the animal or into the products obtained from animal. Therefore, along with an estimate for digestible nutrients, a total nutritional assessment is used (caloric content).
Sulfur
The sulfur is vital for the body of the animal. In the body of animals is mainly in the form of complex organic compounds - amino acids of protein. In the body of animals, sulfur is 0.12-0.15%, most of it focuses in the hairproof, horny shoe, skin. The sulfur is also included in insulin (pancreatic hormone) and thiamine (vitamin B1).
Relatively a lot of sulfur in grain cereals and legumes, meadow and alfalon hay, the fraud. All food rich in protein contains more sulfur than poor them.
The need for sulfur sheep and livestock is 0.25-0.4% of the dry matter of the feed diet. For example, a dairy cow of sulfur needs 25-50 g per day depending on the daily fishing, calves up to 6 months - 3-10, young - 13-25, depending on the living mass and growth; Sheep: adults- 3-9, lambs - 2-3 g per day. The need for sheep in sulfur depends mainly from Nastrig's wool.
The sulfur improves the digestion of cellulose and supports the biosynthesis of the vitamins of the group V. Symptoms of the lack of sulfur in the body are the loss of appetite, loss of part of the hair cover and dull eyes. Many animal feed can serve as a source of sulfur, for example, milk in various form, etc.
It carries out its physiological role in the body through amino acids - cystine, methionine, taurine, glutathione, thiamine, which includes.
Amino acid protein
Cystin
An important amino acid containing sulfur. It is a powerful antioxidant that liver uses for neutralization of destructive free radicals.
Strengthens the connecting tissues and enhances the antioxidant processes in the body.
Promotes healing processes, stimulates the activity of white blood cells, helps reduce pain in inflammation.
Important acid for leather and hair.
Need to protect against chemical toxins.
Metionine
One of the essential amino acids containing sulfur. Important for many functions of the body, including the production of immune cells and the functioning of the nervous system. It is a powerful antioxidant and important to preserve a healthy liver.
Predecessor of Custina and Creatine.
It may increase the level of antioxidants (glutation) and reduce cholesterol.
It helps to remove toxins and restore liver and kidney tissue.
methionine prevents skin diseases.
useful in some cases allergies, since reduces the allocation of histamine.
Taurin
One of the most important, useful and safe amino acid additives is Taurine, widely known due to its favorable effect on the cardiovascular system. The body can produce taurine from cysteine \u200b\u200bwith vitamin B6.
Helps the absorption and destruction of fats.
Taurine, which is present in the organs of the central nervous system, the retina of the eye, skeletal muscles and in the heart muscle, is useful in the treatment of cardiovascular diseases and some eye diseases.
Taurine functions in electrically active tissues, such as the brain and heart, and helps stabilize cell membranes.
It is believed that this amino acid has some antioxidant and cleansing effect.
With the help of zinc, Taurine contributes to the circulation of some minerals inside and outward cells and thus participates in the production of nerve impulses.
Glutathione
Glutathione is not a protein-building amino acid, this is a mixture of amino acid chains.
Glutathione forms enzymes, such as glutathione peroxidase.
It is important for life and is present in all cells of plants and animals.
It is part of the nutrient formulas, as well as additives that have a cleansing effect on the body, removing certain toxins
Tiamine (B1)
Synonyms: Aneuryl, Aneuryrene, Bevemen, Beanva, Berin, Betaxine, Betimine, Bitevan, Orizanin, etc.
Participates in carbohydrate exchange, regulates the functions of the nervous system, cardiac activity. The absorption of vitamin occurs in the intestines, and in tissue cells it turns into cocarboxylase.
Protects cell membranes from toxic exposure to product peroxidation products.
In vitamin B1 not all pets need. In ruminant animals, thiamine is formed using some bacteria living in the RubE. However, poultry, rabbits, pigs and horses are very sensitive to the lack of this vitamin.
And those animals that do not receive and do not produce independently vitamin B1, often get into polyneurite. Under polyneurite, as a rule, a disorder of coordination of movements, a shaky gait, accompanied by rotational motions and paralymps, is reproduced by microflora and the simplest in the refamps of ruminant animals. It is well absorbed, but in an intestinal alkaline medium is destroyed, so it is used after feeding or parenterally with hypo - and avitaminosis B1, polyneuritis of different origin, the muscles of the stomach and intestines, to accelerate the growth of animals and birds. Prescribed inside, subcutaneously and intramuscularly.
The need for vitamin B1 per 1 kilogram of feed from chickens is 1 milligram, in pigs 3 milligrams. With therapeutic goal, doses are 3-8 times large. Doses of intramuscularly and subcutaneously (d): horses and cattle - 0.1-0.3, small cattle and pigs - 0.005-0.06, calves - 0.01-0.06, dogs - 0.001-0, 01, chirms and geese - 10-25 mg; Chickens - 1-2 mg on the head per day. Inside: chickens - 3-4 mg, piglets - 25-40 mg.