TABLE OF CONTENT

CONTENT PAGE Definition & structure of protein -----------------------------------------1

Properties of protein ---------------------------------------- 2

Amino acids &Polypeptides ------------------------------------------ 3

Haemoglobin ------------------------------------------- 4

Collagen and myolglobin ------------------------------------------- 5

IMPORTANCE OF PROTEIN ---------------------------------6

Proteins are macromolecules because of their very high weights. There are chains like molecules produced by joining a number of small units of amino acids called monomers. It is any of a large number of organic compounds that make up living organisms and are essential to their functioning. First discovered in 1838, proteins are now recognized as the predominant ingredients of cells, making up more than 50 percent of the dry weight of animals. Protein molecules range from the long, insoluble fibers that make up connective tissue and hair to the compact, soluble globules that can pass through cell membranes and set off metabolic reactions. They are all large molecules, ranging in molecular weight from a few thousand to more than a million, and they are specific for each species and for each organ of each species. Humans have an estimated 30,000 different proteins, of which only about 2 percent have been adequately described. The following is the structure of the protein. H I

COO - C CH2 NH3 (PROTEIN STRUCTURE) I H3N The structure of protein is more complicated than the other molecules, they are therefore classified into 4 basic levels of organization. The primary structure is the most basic level of protein structure; it is the linear sequence of amino acids. Different sequences of the acids along a chain, however, affect the structure of a protein molecule in different ways. The main mode of linkage of the amino acids in proteins is the peptide bond which links the -carboxyl group of one amino acid residue to the amino group of the other. Secondary structure are as a result of forces such as hydrogen bonds, disulfide bridges, attracts between positive and negative charges, and hydrophobic and hydrophilic linkages cause a polypeptide chain to coil or fold into alpha helix and the beta pleated sheet. When forces cause the molecule to become even more compact, as in globular proteins. Tertiary protein structure is the folding of the long helix chain into a compressed structure giving a globular shape. Quaternary structure when a protein is made up of more than one polypeptide chain to form a functional protein, as in hemoglobin and some enzymes. It consists of 4 subunits two of which are alpha and beta. 1 Proteins have both physical and chemical properties. The following are Physical Properties : It is colourless and tasteless. Shapes range from simple crystalloid to fibrillar structure. Have high molecular weight that ranges from 5 x 10 3 to 1.0 x 106 It is colloidal in nature. It can be denatured by PH, Heat, Chemical and radiation. Proteins are amphoteric, meaning they exibit both acidic and basic properties. Solubility of properties is influenced by PH and salts. Chemicals Properties include the following: a) By proteolytic enzymes undermild

conditions of temperature and acidity enzymes as pepsin and trypsin hydrolyze proteins. b) Hydrolysis reaction By acidic agents proteins reach with acid under specified conditions such as temperature between 100C - 110C to yield amino acids. c) By alkaline agents may also hydrolyze proteins under certain conditions. However this method is not preferred because it leads to the destruction of certain amino acids. It also leads to racemization (loss of optical activity) Reaction with alkalies (salt formation) proteins reacts using their COOH group with alkalies giving salts as products. Ions such as Na + and Ca+ are usually involved in this reaction. H H E C-COOH + BOH R C COOB + H2O + NH 3 NH+3 Proteins Base Salt Water Reaction with alcohols (Etherification) - The COOH group of a protein being acidic can react with an alcohol to produce an ester. R CH COOH + HOC2H5 R CH COO C2H5 + H20 NH2 NH2 Proteins Alcohol Ester Water Reaction involving NH2 Group.The amide end of proteins reaction with mineral acids to produce salts. R CH COOH + HCL R CH COOH NH2 NH2 HCL 2 AMINO ACIDS are important class of organic compounds that contain both the amino (NH2) and carboxyl (COOH) groups. Of these acids, 20 amiono acids serve as the building blocks of proteins Known as the standard, or alpha, amino acids, they comprise alanine, arginine, asparagine, aspartic acid, cysteine,

glutamic acid, glutamine, glycine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, proline, serine, threonine, tryptophan, tyrosine, and valine. All 20 are constructed according to a general formula: H I RC - COOH (AMINO ACID) I NH2 As the formula shows, the amino and carboxyl groups are both attached to a single carbon atom, which is called the alpha carbon atom. Attached to the carbon atom is a variable group (R); it is in their R groups that the molecules of the 20 standard amino acids differ from one another. It is usual to write a peptide chain with a free amino group at the beginning and a free carboxyl group at the end. When a living cell makes protein, the carboxyl group of one amino acid is linked to the amino group of another to form a peptide bond. The carboxyl group of the second amino acid is similarly linked to the amino group of a third, and so on, until a long chain is produced. This chainlike molecule, which may contain from 50 to several hundred amino acid subunits, is called a polypeptide. The structure below is a peptide bond. O II - C-C-N-C(PEPTIDE BOND) I H Each peptide chain is of considerable length and may possess from 50 to millions of amino acid unit. Depending on the number of amino acid molecules composing a chain the peptide may be termed as a dipeptide, a tripeptide. If a peptide is made up of not more than 10 amino acid is called an oligopeptide, beyond that it is a polypeptide. 3 Collagen is a protein synthesized by connective tissue cells. It is the most abundant protein in vertebrates. Collagen molecules are secreted into the extracellular space to become part of the

connective tissue matrix. The genetically distinct collagen molecules in skin, bones, tendons, blood vessels and corneas impart to these structures many of their special properties for example the tensile strength of tendons and the transparency of corneas. Collagen is composed of three left handed polypeptide helices that are twisted around each other to form a right handed triple helix. Type 1 collagen molecules found in teeth, bone, skin and tendons, are about 300mn long and approximately 1.5mn wide. There are 20 major families of collagen molecules. Approximately 90% of the collagen found in humans is type 1 Glycine constitutes approximately one-third of the amino acid residues. Proline and 4 hydroxyproline may account for as much as 30% of a collagen molecules amino acid composition. Specific proline and lysine residues in collagens primary sequence are hydroxylated within the rough ER after the polypeptides have been synthesized. Collagens amino acid sequence primary consists of large number of repeating triplets with the sequence of Gly X Y, in which X and Y are often proline and hydroxyproline. Hydroxylysine is also found in the Y Position. Collagen makes up bone, skin, tendons, and cartilage, is the most abundant protein found in vertebrates. The molecule usually contains three very long polypeptide chains, each with about 1000 amino acids that twist into a regularly repeating triple helix and give tendons and skin their great tensile strength. When long collagen fibrils are denatured by boiling, their chains are shortened to form gelatin. 4

HAEMOGLOBIN Haemoglobin is a roughly spherical molecule found in red blood cells where its primary function is to transport oxygen from the lungs to every tissue in the body. The HbA is composed of two - chains and two chain. The HbA molecule is commonly designated 2 2. There is another type of adult hemoglobin. Approximately 2% of human haemoglobin is HbA, which contains 8 delta chains instead of chains. Before birth, several additional haemoglobin polypeptides are synthesized. The (epsilon) chain, which appears in early embryonic life, and the Y chain found in the foetus closely resemble the chain. Because both 2 2 and 2 Y2 haemoglobins have a greater affinity for oxygen than does 2 2 (HBA), the foetus can preferentially absorb oxygen from the maternal blood stream. Although three dimensional configurations of myoglobin and the - and chains of haemoglobin are very similar, their amino acid sequences have many differences. The four chains of haemoglobin are arranged in two identical dimmers, designated as , , and 2 2. Each globin polypeptide has a heme binding unit similar to that, for myoglobin. Although both myoglobin and haemoglobin bind oxygen reversibly, the latter molecule has a complex structure and more complicated binding properties. The numerous non covalent interactions (mostly hydrophobic) between the subunits in each dimer remain largely uncharged when haemoglobin inter converts between its oxygenated and deoxygenated forms. Myoglobin is found in high concentration in skeletal and cardiac muscle, gives these tissues their characteristic red colour. Diving mammals such as whales, which remain submerged for long periods, posses high myoglobin concentrations in their muscles. Because of the extremely high concentration of myoglobin, such muscles are typically brown The protein component of myoglobin, called globin is a single polypeptide chain that contains eight sections of - helix. The folded globin chain forms a crevice that almost completely encloses a heme group. Free heme [ Fe2+ ]. Has a high affinity and is irreversibly oxidized to form hematin [ Fe 3+]. Hematin can not bind O2. Non covalent interactions between amino acid side chains and the non polar porphyrin ring within the oxygen binding crevice decrease hems affinity for O 2. The decreased

affinity protects Fe2+ from oxidation and allows for the reversible binding of O2. All of the heme interacting amino acids are non polar with the exception of two histidines, one of which binds directly to the heme iron atom. The other stabilizes the oxygenbinding site. 5 Proteins are of utmost significance to biological systems. These are most critical to life and perform various functions. Some of their roles are:Most plants and microorganisms are able to use inorganic compounds to make all the amino acids they require for normal growth. Animals, however, must obtain some of the standard amino acids from their diet in order to survive; these particular amino acids are called essential. Essential amino acids for humans include lysine, tryptophan, valine, histidine, leucine, isoleucine, phenylalanine, threonine, methionine, and arginine. They are found in adequate amounts in protein-rich foods from animal sources or in carefully chosen combinations of plant proteins. Many proteins act as catalysts, thus enhancing the rate of chemical reactions to such extents as needed by the living cells. The fibrous proteins serve as components of the tissues holding the skeletal elements together Collagen is a structural unit of connective tissues. The nucleon-proteins serve as carriers of genetic characters and hence govern inheritance of traits. Proteins also perform transport functions. Many compounds enter the cells and accumulate inside at much higher concentrations than expected from diffusion alone. These changes require the input of energy and are usually termed active transport. The mechanism of active transport involves proteins either as catalyst or as adsorbents or as both. Various protein hormones are known. These regulate the growth of plants and animals, besides controlling many other physiological functions.

Under conditions of non-digestion and no chances of denaturation, the proteins accumulate inside the cells and produces toxicity. Bacteria toxins are poisonous substances produced by some disease causing bacteria e.g. Botulism caused by a toxin in animals. Blood plasma which is obtained after removal of the blood cells by centrifugal action is essentially a solution of protein in water. Proteins are also nutritive in function. Proteins act as nutrient source for most amino acids, particularly in man and other animals. Proteins are good buffers because of the various charged groups on the side chains of the amino acids. 6 Proteins also have an osmotic role. Because they are large molecules in solution they increase the osmotic pressure e.g. inside cells making them turgid. They play a role in blood clotting when they exist as fibrinogen. They play a role in vision when they exist as optician. They play a role as hemoglobin such as oxygen transport in the body. Animal proteins, found in such food as eggs, milk, meat, fish, and poultry, are considered complete proteins because they contain all of the essential amino acids our bodies need. Plant proteins, found in vegetables, grains, and beans, lack one or more of the essential amino acids. However, plant proteins can be combined in the diet to provide all of the essential amino acids. A good example is rice and beans. Each of these foods lacks one or more essential amino acids, but the amino acids missing in rice are found in the beans, and vice versa. So when eaten together, these foods provide a complete source of protein. Thus, people who do not eat animal products can meet their protein needs with diets rich in grains, dried peas and beans, rice, nuts, and tofu, a soybean product.

REFERENCES 1. Biology. Peter Raven and George Johnson by McGraw Hill Companies, (1999), New York NYIOO2O USA.

2. Biochemistry, Trudy Mickee ental, (2003), by McGraw Hill Companies, New York USA

3. chem4kids.com/Biochemistry/Enzymeregulation.

4. BURTON. S.C.(1988): UNDERSTANDING BIOLOGY HARCORT JAVANOVIEL INC.

An enzyme is substance produced by living organism that act as a catalyst to bring about a specific biochemical reaction. The function of enzymes is to speed up the rate of reaction. The following are Properties of Enzymes Specificity - there are several types of substrate specificity. Absolute Substrate Specificity This is where the enzyme has only one type of substrate it can work on. An example of an enzyme that displays absolute substrate specificity is Glucose 6 Phosphate Glucose 6 P Glucose + Pi Relative Group Specificity Here the enzyme will catalyze reactions that involve a broad range of substrates. An example of an enzyme with relative group specificity is Hexokinase. i) Glucose + ATP Glucose 6 P + ADP. ii) Fructose + ATP Fructose 6 P + ADP Product They lead to the formation of only one product. Protein Nature The majority of enzymes are protein in nature.

This means that all factors that affect the structure of proteins, i.e. temperature, PH Ionic strength, organic solvents, will affect structure and function of enzymes. Being proteins, they are coded for by DNA. They are catalysts. Their presences do not alter the nature or properties of the end product of the reaction. They are very efficient, such that a very small amount of catalyst brings about the change of a large amount of substrate. For example, one molecule of the enzyme catalase can catalyse the decomposition of about 600 thousand molecules per second of hydrogen peroxide to water and oxygen at body temperature. The enzyme catalyzed reaction is reversible. Their activity is affected by PH, temperature, substrate concentration and enzyme concentration. Enzymes lower the activation energy of the reactions they catalyze. Enzymes possess active sites where the reaction takes place. These sites have specific shapes 1 SPECIFICITY OF ENZYMES With few exceptions, the enzymes are specific in their action. Their specificity lies -in the fact that they act on one specific type of substrate molecule or -On a group of structurally related compounds or - even on only one of the two optical isomers of a compound or on only one of the two geometrical isomers. Specificity comes about as a result of special conjunction between the active site of an enzyme and the active site of a substrate. E S

The two active sites must give a precise fit if an enzyme is to act on a given substrate. An active site is a three dimensional crevicle with a specific geometry on the surface of either on an enzyme or substrate. CATALYSIS A universal feature of all enzymatic reactions is the virtual absence of any side products. They act catalytically and accelerate the rate of chemical reactions occurring in plant and animal tissues. They do not normally participate in these reactions or if they do so, at the end of the reactions, they are recovered as such without undergoing any qualitative or quantitative change. This is the reason why they, in small amounts, are capable of catalyzing the transformation of a large quantity of substrate. ENZYME REGULATION - this is where sometimes there is need to be controlled. An organism can create its own molecules to slow down and stop the activity of enzymes and proteins. At other times, enzymes can be controlled by poison and contaminants, such as herbicides. What affects enzyme activity are as follows:Temperature . 2 Proteins change shape as temperatures change. Because so much of an enzymes activity is based its shape, temperature changes can mess up the process and the enzyme cannot work. High temperature will cause the enzyme to denture and have its structure start to break up. Activators: Sometimes you need an enzyme to work faster your body can then create activators. At other times, you might eat something that plays the role of an activator. Activators make enzymes work harder and faster. Hormones can trigger responses that activate enzymes. PH Levels. The acidity of the environment changes the shape of protein in the same way that temperature does. An increase in acidity near an enzyme can cause its shape to change. The polar

and non-polar amino acids start to twist. If there is enough of a change the protein could unravel and become totally infective. Inhibitors: are opposite of activators. Inhibitors either slow down or stop the activity of an enzyme. They often bond to the protein, changing the overall shape of the enzyme. When the shape changes, the enzyme will not work the same way. A nasty example of an inhibitor is snake venom or may be nerve gas from world war, 1. Enzymes are classified according to mode of action that they provide as follows:1. Oxidoreductases This is a class of enzymes that catalyses reactions where there is transfer of electrons from one molecule to another. CH3 CH3 + CHOH + NAD CO + NAD (+H+) COO COO Pactate Nicotinamide Pyruvate Reduced NAD+ Adenine Dinicteodite 3

2. Transferases Its a group of enzymes that catalyze transfer of group of atoms e.g. acetyl amino, phosphate formation of citrate from oxalacetate CH2COO CO.COO + CH3 + H2O C. OH.COO + + HS.COA + H CH2COO COS.COA Oxalacetate Acetyl COA Citrate CO Enzyme A 3. Hydrolases

These are enzymes that catalyze hydrolytic . Cleovage. e.g. Cleovage of fats and protese CH2 .O. COR1 CH2OH CH. O. CO. R1 + H2O CH. CO. R2 + R3 COOH + R, COOH CH2. O. CO. R1 CH2OH Triglyceride Monocylylycerol (Triacylglcerol) 4. Lyases Are enzymes that catalyzes non hydrolytic reaction or catalyze reactions where no water is involved (non-hydrolytic decomposition e.g decarboxylation and deamination. Pyruvate decarboxylase is a lyase enzyme responsible for convension of 2 O X O acid to an aldehyde and CO 2. R R C: O CHO + CO2 COOH Z OXO Acid Aldehde Carbondioxide 5. Isomerases These are enzymes that catalyze intramolecular rearrangement in optical and positional isomers. Typical of this class of enzymes are epimerase such as uridine diphosphate glucose 4 epimerase which catalyze damage of fourth cation of glucose to produce galactose. 6. Ligases Are enzymes that catalyze synthesis involving breaking of ATP or similar triphosphate to provide energy for reaction? 4 KINETICS OF ENZYMES This is the quantitative study of enzyme; catalysis provides information about reaction rates. A simple enzymatic reaction might be written E + S ES EP E + P Where, E, S and P represent enzymes, substrate and product, respectively. ES and EP are complexes of the enzyme with substrate and with the product, respectively. For a better understanding of the kinetics of a chemical reaction, the two terms, reaction, Equilibria and reaction rates must be

differentiated. The function of a catalyst is to increase the rate of a reaction. Catalysts do not affect reaction Equilibria. Any reaction such as S P can be described by a reaction coordinate diagram. Transition state (#) Energy require to reverse the reaction S G of both energy S substrate of that Ground of product Reaction Coordinate Therefore the productat lower state of energy Free energy diagram for a simple chemical reactions, S P content though all are at ground state Energy in biological system is described in terms of free energy, G. The diagram shows that in its normal stable form or ground state, any molecule contains a specific amount of free energy. Chemists express the free energy change for this reacting system under standard set of conditions (temperature, 298 k. partial pressure of gases, each latm or 101.3 Kpa; PH = O; concentration of solutes, each (1M) and call this as standard free energy change, G. Because biological systems commonly, involve H+ concentrations far from 1 M, biochemistry define a constant G; the standard free energy change at PH 7.0. The equilibrium between S and P reflects the difference in the free energy of their ground states. In the figure above, the free energy of the ground state of P is lower than that of S, hence G for the reaction is negative and the equilibrium favours P. This equilibrium is not affected by any catalyst. A favorable equilibrium, however, does not mean that S P conversion is G# S G P
#

fast. The rate of reaction in fact, depends on an entirely different parameter. Their exists an energetic barrier between S and P that represents the energy required for alignment of reacting group, bond rearrangements and other charged needed for the reaction to occur in either direction. To undergo reaction, the molecules must overcome this barrier or energetic hill and therefore must be raised to a higher energy level. At the top of energy hill is a point at which decay to the S or P state is equally probable which is downhill either way. This is called the transition state and should not be confused with a reaction intermediate. It is simply a moment of fleeting molecules in which certain events (bond breakage, bond formation, charge development etc) have proceeded to decide the future course of the reaction. i.e. a collapse to either substrate or product. The difference between the energy levels of the ground state and the transition state is called the Gibbs free energy of activation or simply activation energy and is symbolized G#. The double dagger (#) denotes a thermodynamic quantity of a transition. The rate of reaction reflects this activation energy; a higher activation energy corresponds to a slower reaction. Reaction rates can be increased by rising the temperature, thereby increasing the number of molecules with higher energy to overcome this energy barrier. As and alternate, the activation energy can be lowered. Thus catalysts enhance reaction rates by lowering activating energies.

G G EP G

S ES Ground state

Reaction coordinate 6 Catalysts affect the reaction rates, not the reaction Equilibria. The enzyme is not consumed in the process, and the equilibrium

point remains unaffected. However, the reaction reaches equilibrium much faster when the appropriate enzyme is present because the rate of the reaction is increased.

REFERENCES

1. Biology. Peter Raven and George Johnson by McGraw Hill Companies, (1999), New York NYIOO2O USA.

2. Biochemistry, Trudy Mickee ental, (2003), by McGraw Hill Companies, New York USA

3. chem4kids.com/Biochemistry/Enzymeregulation.

4. BURTON. S.C.(1988): UNDERSTANDING BIOLOGY HARCORT JAVANOVIEL INC.

Carbohydrate can be defined as polyhydroxy aldehyde or polyhydroxy ketone. It is any of a large group of compounds in which hydrogen and oxygen, in the proportions in which they exist in water, are combined with carbon; the formula of most of these compounds may be expressed as Cn(H2O)n. Structurally, however, these compounds are not hydrates of carbon, as the formula would seem to indicate. They are produced by green plants and by bacteria using the process known as photosynthesis, in which carbon dioxide is taken from the air by means of solar energy to yield the carbohydrates as well as all the other chemicals needed by the organisms to survive and grow. The carbohydrate group consists principally of sugar, starch, dextrin, cellulose, and glycogen, substances that constitute an important part of the human diet and that of many animals. Carbohydrates are classified in 3 groups namely Monosaccharides Oligosaccharide polysacchrides The simplest of them are the simple sugars, or monosaccharides, which contain either an aldehyde or a ketone group. The most important is glucose. They are simple sugars which possess a free aldehyde (CHO) or ketone (CO) group and 2 or more hydroxyl (-OH) groups. Monosacchrides cannot be hydrolysed into smaller units. Two monosaccharide molecules joined together by an oxygen atom, with the elimination of a molecule of water, yield a disaccharide. Disaccharide have the following formula Cn(H2O) n-1 of which the most important are sucrose lactose, and maltose. It can be classified into: Reducing sugar such as Lactose, maltose and celluloce Non reducing sugars such as sucrose, Trehalose. Free disaccharide is found more often in plants than animals. Sucrose is the chief constituent of sugarbeet and sugarcane. It

can be hydrolysed into constituent monosaccharide by acid or by an enzyme called invertase. Polysaccharides have this formula ( C6H10O2)X, these are enormous molecules made up of one type or several types of monosaccharide unitsabout 10 in glycogen, for example; 25 in starch; and 100 to 200 in cellulose. Some common examples are: 1 Homopolysacchrides which include starch, glycogen, inulin,cellulose,pectin and chitin. Heteropolysaccharides which include hyaluronic acid, and chondroitin. Within living organisms, carbohydrates serve both essential structural and energy-storage functions. In plants, cellulose and hemicellulose are the main structural elements. In invertebrate animals, the polysaccharide chitin is the main component of the exoskeletons of arthropods. In vertebrate animals, the cell coatings of connective tissues contain carbohydrates. Cell membranes are rich in glycoproteins. Glycoprotein is a conjugated protein having a carbohydrate component. These contain oligosaccharide chains attached to polypeptide side. NH I H-CCH3 I C=O N-H I H.C-CH3

CH2OH I I C=O HO I N-H CH2OH I O O OH C=O C=O I CH3 Glycoprotein serves several roles in the body. Some glycoprotein is released in the blood, while others carry blood group. Those embedded in the plasma membrane carry out a variety of functions, which include transportation of large water soluble molecules such as sugars and certain amino acids. 2 Glycoprotein also serve in part to identify the cell as belonging to a unique organism, enabling the immune system to detect foreign cells, such as invading bacteria, which carry different glycoproteins. Below is a structure of one of the glycoprotein. The above segment is a recurring glycol-tripeptide unit. Each disaccharide unit, composed of - 1,3 linked residuesof galactose and N acetylgalactosamine is attached to the polypeptide chain by a glucosidic linkage to threonine residue. Glycolipids are lipids with a carbohydrate attached. Their role is to provide energy and also serve as markers for cellular. They are membrane components composed of lipids that are covalently bonded to monosaccharaides. Can also be said to be fats that have attached carbohydrate groups called glycan. Glycolipids are present ubiquitously in cell surface membranes. They have polar heads and non-polar tails. They may act as I I OH NH I I O-CH- CH I I CH H I I O

receptor site for chemical signals. With are also involved in sticking the correct cells together in tissues. Sterols are composed of complicated molecules. Each containing 20 or more carbon atoms in an interlocking or fused ring structure. Cellulose is an insoluble substance that is the main constituent of plant cell walls and of vegetable fibbers such as cotton. It is a polysaccharide. It is a long chain of linked sugar molecules that gives wood its remarkable strengthen. Cellulose is normally combined with woody, fatty, or gummy substances. With some exceptions among insects, true cellulose is not found in animal tissues. Microorganisms in the digestive tracts of herbivorous animals break down the cellulose into products that can then be absorbed. Cellulose is insoluble in all ordinary solvents and may be readily separated from the other constituents of plants. Depending on its concentration, sulfuric acid acts on cellulose to produce glucose, soluble starch, or amyloid. It is a form of starch used for the then exposed to the fumes of carbon disulfide, the solution yields films and threads. Rayon and cellophane are cellulose regenerated from such solutions. Cellulose acetates are spun into fine filaments for the manufacture of some fabrics and are also used for photographic safety film, as a substitute for glass, for the manufacture of safety glass, and as a molding material. 3 Cellulose ethers are used in paper sizings, adhesives, soaps, and synthetic resins.

O
CH2OH

CH2OH

CH2OH

CH2OH

CH2OH

CH2OH

o OI

CH2OH

OI O I O I OI
CH2OH

I O I OI
CH2OH

O I OI
CH2OH

O I

CH2OH

CH2OH

Carbohydrates are important in that:

Glucose is a preferred energy source of man tissue especially the brain. It is the primary fuel for living cells. In animals , glucose is the preferred energy source of brain cells and that have few or no mitochondria such as erythrocytes, cells that have a limited oxygen supply. Such as those in the eyeball, also use large amounts of glucose to generate energy dietary source include plant starch and the disaccharide, maltose and sucrose. Nitrocellulose is used in the production of motion picture film, cement, guncotton, celluloid, and similar kinds of plastics. Starch is used in the preparation of foods for livestock and humans; pectin, a jelling agent; gum arabic; and agar, used in the production of adhesive materials, sizing materials, and emulsions. Gum arabic is also used in demulcent medicines. Agar, a With mixtures of nitric and sulfuric acids, cellulose forms a series of flammable and explosive compounds known as cellulose nitrates, or nitrocelluloses. Pyroxylin, also called collodion cotton, is a nitrate used in various lacquers and plastics; another, collodion, is used in medicine, photography, and the manufacture of artificial leather and some lacquers. A third nitrate, guncotton, is a high explosive. Cellulose is a popular food additive used as astabiliser. Carbohydrate can be converted into viscose rayon, acetate rayon, and paper products. Constituent of some laxatives is also used as a thickening agent in food and as a medium for bacterial culture. Hemicellulose is used to modify paper during its manufacture. The carbohydrate dextran is a polysaccharide used in medicine as a blood-plasma-volume expander to counteract acute shock. 4 Another carbohydrate, heparin sulfate, is a blood anticoagulant. Chains Plants use starch and animals use glycogen to store energy, when the energy is needed, the carbohydrates are broken down by enzymes. Carbohydrates are used in the manufacture of fabrics, photographic film, plastics, and other products.

Galactose is hexose found mostly commonly as a component of disaccharide lactose or milk sugar. Galactose is necessary for synthesis a variety of biomolecules.