Protein

Protein Functions:
-The unique shapes of proteins enable them to perform their various tasks in the body.
-Some form hollow balls that can carry and store materials within them, and some, such as
those of tendons, are more than ten times as long as they are wide, forming strong, rod like
structures.
-Some polypeptides are functioning proteins just as they are;others need to associate with
other polypeptides.
-Some proteins require minerals to activate them. One molecule of hemoglobin made of four
associated polypeptide chains, each holding the mineral iron.

Protein Denaturation: When proteins are subjected to heat, acid or other conditions that
disturb their stability, they undergo denaturation.
-They uncoil and lose their shapes and also lose their ability to function.
-Denaturation is irreversible:
-the hardening of an egg when it is cooked. -the curdling of milk when acid is added.
-the stiffening of egg whites when they are whipped

Digestion of Protein: Proteins in foods do not become body proteins directly. Instead,they
supply the amino acids from which the body makes its own proteins.
In the Stomach:
-The major event in the stomach is the partial breakdown (hydrolysis) of proteins.
-Hydrochloric acid uncoils (denatures) each protein’s tangled strands so that digestive
enzymes can attack the peptide bonds.
-The hydrochloric acid also converts the inactive form of the enzyme pepsinogen to its active
form, pepsin.
-Pepsin cleaves proteins—large polypeptides—into smaller polypeptides and some amino
acids.
In the Small Intestine:
-When polypeptides enter the small intestine, several pancreatic and intestinal proteases
hydrolyze them further into short peptide chains, tripeptides, dipeptides, and amino acids.
-Then peptidase enzymes on the membrane surfaces of the intestinal cells split most of the
dipeptides and tripeptides into single amino acids.
-Only a few peptides escape digestion and enter the blood intact.

Protein Absorption: -A number of specific carriers transport amino acids (and some
dipeptides and tripeptides) into the intestinal cells.
-Once inside the intestinal cells, amino acids may be used for energy or to synthesize needed
compounds. Amino acids that are not used by the intestinal cells are transported across the
cell membrane into the surrounding fluid where they enter the capillaries on their way to the
liver.
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Proteins in the Body:
Sequencing Errors: The sequence of amino acids in each protein determines its shape and
function. If a genetic error alters the amino acid sequence of a protein, or if a mistake is made in
copying the sequence, an altered protein will result, sometimes with dramatic consequences.
-Hemoglobin offers one example of such a genetic variation.

Roles of Proteins:
1-As Building Materials for Growth and Maintenance: proteins form the building blocks of
muscles, blood, and most body structures.
-To build a bone or a tooth,cells first lay down a matrix of the protein collagen and then fill it
with crystals of calcium, phosphorus, magnesium, fluoride, and other minerals.
-Collagen also provides the material of ligaments and tendons and the strengthening glue
between the cells of the artery walls that enables the arteries to withstand the pressure of the
blood with each heartbeat.
Proteins are also needed for replacing dead or damaged cells,The life span of a skin cell is only
about 30 days. As old skin cells are shed, new cells made largely of protein grow from
underneath to replace them.
-Muscle cells make new proteins to grow larger and stronger in
response to exercise.
-Cells of the GI tract are replaced every few days.

2-As Enzymes: Some proteins act as enzymes, eg. digestive enzymes

-Enzymes not only break down substances, but they also buildEnzymes not only break down
substances, but they also build substances (such as bone) and transform one substance into
another (amino acids into glucose).

3-As Hormone: The body’s many hormones are messenger molecules, and some hormones are
proteins.
-The blood carries the hormones from these glands to their target tissues, where they elicit the
appropriate responses to restore and maintain normal conditions.
-The hormone insulin provides an example

4-As Regulators of Fluid Balance:

-Blood proteins such as albumin and globulin help to maintain the body’s fluid balance.
(proteins attract water from leaking to the interstitial space )-
-the body’s fluids are contained inside the cells (intracellular) or outside the cel (extracellular).
- Extracellular fluids, can be found either in the spaces between the cells (interstitial) or within
the blood vessels (intravascular).
 Protein
4-As Regulators of Fluid Balance:
-The fluid within the intravascular spaces is called plasma (essentially blood without its red
blood cells).
-Fluids can flow freely between these compartments, but being large, proteins cannot. Proteins
are trapped primarily within the cells and to a lesser extent in the plasma.
-The exchange of materials between the blood and the cells takes place across the capillary
walls, which allow the passage of fluids and a variety of materials.
-Some plasma proteins leak out of the capillaries into the interstitial fluid between the cells,
but can reenter the system via the lymphatic system.
-If plasma proteins enter the interstitial spaces faster than they can be cleared, fluid
accumulates (because plasma proteins attract water) and causes swelling. Swelling due to an
excess of interstitial fluid is known as edema.
-The protein-related causes of edema include:
• Excessive protein losses caused by kidney disease or large wounds (such as extensive burns)
• Inadequate protein synthesis caused by liver disease
• Inadequate dietary intake of protein

As Acid-Base Regulators:
-Proteins also help to maintain the balance between acids and bases within the body fluids.
-In an acid solution, hydrogen ions (H+) abound; the more hydrogen ions, the more
concentrated the acid. Proteins,which have negative charges on their surfaces, attract
hydrogen ions, which have positive charges.
-By accepting and releasing hydrogen ions, proteins maintain the acid-base balance of the
blood and body fluids.
-The blood’s acid-base balance is tightly controlled. The extremes of acidosis and alkalosis lead
to coma and death,largely because they denature working proteins. example:denatured.
hemoglobin loses its capacity to carry oxygen.

As Transporters: Some proteins move about in the body fluids, carrying nutrients and other
molecules.
-The protein hemoglobin carries oxygen from the lungs to the cells.
-The lipoproteins transport lipids around the body. Special transport proteins carry vitamins
and minerals.
-Each transport protein is specific for a certain compound or group of related compounds.
-A membrane-bound transport protein helps to maintain the sodium and potassium
concentrations in the fluids inside and outside cells. The balance of these two minerals is
critical to nerve transmissions and muscle contractions; imbalances can cause irregular
heartbeats, muscular weakness, kidney failure, and even death.
 Protein

As Antibodies: Proteins also defend the body against disease.

-When the body detects these invading antigens, it manufactures antibodies, giant protein
molecules designed specifically to combat them.
-The antibodies work efficiently that in a normal,healthy individual, most diseases never have a
chance to get started.Without sufficient protein,the body cannot maintain its army of
antibodies to resist infectious diseases.of antibodies to resist infectious diseases.

As a Source of Energy and Glucose: Without energy, cells die; without glucose, the brain and
nervous system falter.
-Proteins can be sacrificed to provide energy and glucose during times of starvation or
insufficient carbohydrate intake.
-The body will break down its tissue proteins to make amino acids available for energy or
glucose production.
-protein can maintain blood glucose levels, but at the expense of losing lean body tissue.
Other Roles: Proteins form integral parts of most body structures such as
skin, muscles, and bones.
-They also participate in blood clotting and vision. When a tissue is injured, a rapid chain of
events leads to the production of fibrin, a stringy, insoluble mass of protein fibers that forms a
solid clot from liquid blood. Later, more slowly,
the protein collagen forms a scar to replace the clot and permanently heal the wound.
-The light-sensitive pigments in the cells of the eye’s retina are molecules of the protein opsin.
-Opsin responds to light by changing its shape, thus initiating the nerve impulses that convey
the sense of sight to the brain.
 Protein
Preview of Protein Metabolism:
Protein Turnover and the Amino Acid Pool: Within each cell, proteins are continually being
made andbroken down, a process known as protein turnover.
—When proteins break down, they free amino acids. These amino acids mix with amino acids
from dietary protein to form an “amino acid pool” within the cells and circulating blood.
-The rate of protein degradation and the amount of protein intake may vary, but the pattern of
amino acids within the pool remains fairly constant.
-Regardless of their source, any of these amino acids can be used to make body proteins or
other nitrogen-containing compounds, or they can be stripped of their nitrogen and used for
energy.

Nitrogen Balance: Protein turnover and nitrogen balance go hand in hand.

-In healthy adults, protein synthesis balances with degradation,and protein intake from food
balances with nitrogen excretion in the urine, feces, and sweat.
-When nitrogen intake equals nitrogen output, the person is in nitrogen equilibrium, or zero
nitrogen balance.
-Researchers use nitrogen balance studies to estimate protein requirements. If the body
synthesizes more than it degrades and adds protein, nitrogen status becomes positive.

-Nitrogen status is positive in growing infants, children, adolescents, pregnant women, and
people recovering from protein deficiency or illness; their nitrogen intake exceeds their
nitrogen output. They are retaining protein in new tissues as they add blood, bone, skin, and
muscle cells to their bodies.
-If the body degrades more than it synthesizes and loses protein, nitrogen status becomes
negative. Nitrogen status is negative in people who are starving or suffering other severe
stresses such as burns, injuries, infections, and fever; their nitrogen output exceeds their
nitrogen intake. During these times, the body loses nitrogen as it breaks down muscle and other
body proteins for energy.

Using Amino Acids to Make Proteins: or Nonessential Amino Acids

-Cells can assemble amino acids into the proteins they need to do their work. If a particular
nonessential amino acid is not readily available, cells can make it from another amino acid. If an
essential amino acid is missing, the body may break down some of its own proteins to obtain it.
-Using Amino Acids to Make Other Compounds Cells can also use amino acids to make other
compounds. For example, the amino acid tyrosine is used to make the neurotransmitters
norepinephrine and epinephrine, which relay nervous system messages throughout the body.
 Protein

-Tyrosine can also be made into the pigment melanin, which is responsible for brown hair, eye,
and skin color, or into the hormone thyroxin, which helps to regulate the metabolic rate.
-For another example, the amino acid tryptophan serves as a precursor for the vitamin niacin
and for serotonin, a neurotransmitter important in sleep regulation, appetite control, and
sensory perception.

Using Amino Acids for Energy and Glucose:

-when glucose or fatty acids are limited, cells are forced to use amino acids for energy and
glucose.
-The body does not make a specialized storage form of protein as it does for carbohydrate and
fat. protein in the body is available only from the working and structural components o the
tissues.
-When the need arises, the body breaks down its tissue proteins and uses their amino acids for
energy or glucose.
-Thus, over time, energy deprivation always causes wasting of lean body tissue as well as fat
loss.
Deaminating Amino Acids:
-When amino acids are broken down (used for energy), they are first deaminated—stripped of
their nitrogen- containing amino groups.
-Deamination produces ammonia, which the cells release into the bloodstream. The liver picks
up the ammonia, converts it into urea (a less toxic compound), and returns the urea to the
blood.
-The production of urea increases as dietary protein increases, until production hits its
maximum rate at intakes approaching 250 grams per day.
-The kidneys filter urea out of the blood; thus the amino nitrogen ends up in the urine.

Using Amino Acids to Make Fat: Amino acids may be used to make fat when energy and protein
intakes exceed needs and carbohydrate intake is adequate.
-The amino acids are deaminated, the nitrogen is excreted, and the remaining carbon fragments
are converted to fat and stored for later use.
-In this way, protein-rich foods can contribute to weight gain.
 Protein

Protein Quality:
-The protein quality of the diet determines how well children grow and how well adults
maintain their health.
-high-quality proteins provide enough of all the essential amino acids needed to support the
body’s work, and low quality proteins don’t.
-Two factors influence protein quality—the protein’s digestibility and its amino acid
composition.

Digestibility: proteins must be digested before they can provide amino acids. Protein
digestibility depends on such factors as the protein’s source and the other foods eaten with it.
-The digestibility of most animal proteins is high (90 to 99 percent); plant proteins are less
digestible (70 to 90 percent for most, but over 90 percent for soy and legumes).
Amino Acid Composition:
-To make proteins, a cell must have all the needed amino acids available simultaneously. The
liver can produce any nonessential amino acid that may be in short supply so that the cells can.
continue linking amino acids into protein strands.
-If an essential amino acid is missing, though, a cell must dismantle its own proteins to obtain it.
Therefore, to prevent protein breakdown, dietary protein must supply at least the nine
essential amino acids plus enough nitrogen- containing amino groups and energy for the
synthesis of the others.
-If the diet supplies too little of any essential amino acid, protein synthesis will be limited.
-The body makes whole proteins only; if one amino acid is missing, the others cannot form a
“partial” protein. An essential amino acid supplied in less than the amount needed to support
protein synthesis is called a limiting amino acid.
Reference Protein: The quality of a food protein is determined by comparing its amino acid
composition with the essential amino acid requirements of preschool age children.
-Such a standard is called a reference protein.
-The rationale behind using the requirements of this age group is that if a protein will
effectively support a young child’s growth and development, then it will meet or exceed the
requirements of older children and adults.
 Protein

High-Quality Proteins:contains all the essential amino acids in relatively the same amounts
and proportions that human beings require; it may or may not contain all the nonessential
amino acids.
-Proteins that are low in an essential amino acid cannot, by themselves, support protein
synthesis. Generally, foods derived from animals (meat, fish, poultry, cheese, eggs, yogurt, and
milk) provide high-quality proteins,
-Proteins from plants (vegetables, nuts, seeds, grains, and legumes)have more diverse amino
acid patterns and tend to be limiting in one or more essential amino acids.
-Some plant proteins are notoriously low quality (for example, corn protein). A few others are
high quality (for example, soy protein).

Complementary Proteins: many vegetarians improve the quality of proteins in their diets by
combining plant-protein foods that have different but complementary amino acid patterns.
-This strategy yields complementary proteins that together contain all the essential amino
acids in quantities sufficient to support health.
-The protein quality of the combination is greater than for either food alone.
-Many people believe that combining plant proteins at every meal is critical to protein
nutrition. For most healthy vegetarians, it is not necessary to balance amino acids at each
meal if protein intake is varied and energy intake is sufficient.
-Vegetarians can receive all the amino acids they need over the course of a day by eating a
variety of whole grains, legumes, seeds, nuts, and vegetables.
-Protein deficiency will develop, however, when fruits and certain vegetables make up the
core of the diet, severely limiting both the quantity and quality of protein.

Health Effects and Recommended Intakes of Protein:

Protein-Energy Malnutrition:When people are deprived of protein, energy, or both, the resul
(PEM).
-Although PEM touches many adult lives, it most often strikes early in childhood. It is one of
the most prevalent and devastating forms of malnutrition in the world, afflicting one of every
four children worldwide.
-Inadequate food intake leads to poor growth in children and to weight loss and wasting in
adults. Children who are thin for their height may be suffering from acute PEM (recent severe
food deprivation), whereas children who are short for their age have experienced chronic PEM
(long-term food deprivation).
 Protein
Classifying PEM :occurs in two forms: 1. Marasmus 2. Kwashiorkor

1-Marasmus: Appropriately named from the Greek word meaning “dying away,”
-marasmus reflects a severe deprivation of food over a long time (chronic PEM).
-Marasmus occurs most commonly in children from 6to18 months of age in all the
overpopulated and impoverished areas of the world.
-Children in impoverished nations simply do not have enough to eat and subsist on diluted
cereal drinks that supply scant energy and protein of low quality; Consequently, marasmic
children look like little old people, just skin and bones.
-Without adequate nutrition, muscles, including the heart, waste and weaken.
-Because the brain normally grows to almost its full adult size within the first two years of life,
marasmus impairs brain development and learning ability.
-The starving child faces this threat to life by engaging in as little activity as possible— not
even crying for food.
- The body musters all its forces to meet the crisis, so it cuts down on any expenditure of
energy not needed for the functioning of the heart, lungs, and brain.
-Growth ceases; the child is no larger at age four than at age two. Enzymes are in short supply
and the GI tract lining deteriorates. Consequently, the child can’t digest and absorb
what little food is eaten.

Kwashiorkor: typically reflects a sudden and recent deprivation of food (acute PEM).
-Kwashiorkor is a Ghanaian word that refers to the birth position of a child and is used to
describe the illness a child develops when the next child is born.
-Kwashiorkor typically sets in between 18 months and two years
-commonly, is precipitated by an illness such as measles or other infection.
-The loss of weight and body fat is usually not as severe as in marasmus, but some muscle
wasting may occur.
-Proteins and hormones that previously maintained fluid balance diminish, and fluid leaks into
the interstitial spaces.
-The child’s limbs and abdomen become swollen with edema,a distinguishing feature of
kwashiorkor.
- A fatty liver develops due to a lack of the protein carriers that transport fat out of the liver.
Marasmus-Kwashiorkor Mix:The combination of marasmus and kwashiorkor is characterized
by the edema of kwashiorkor with the wasting of marasmus.
-Most often, the child suffers the effects of both malnutrition and infections.
-Some researchers believe that kwashiorkor and marasmus are two stages of the same disease.
 Protein
Infections:
-In PEM, antibodies to fight off invading bacteria are degraded to provide amino acids for
other uses, leaving the malnourished child vulnerable to infections.
-Blood proteins, including hemoglobin, are no longer synthesized, so the child becomes
anemic and weak.
-Dysentery, an infection of the digestive tract, causes diarrhea, further depleting the body of
nutrients and fluids.
-In the marasmic child, once infection sets in, kwashiorkor often follows, and the immune
response weakens further.
-The combination of infections, fever, fluid imbalances, and anemia often leads to heart failure
and occasionally sudden death.
-Measles, which might make a healthy child sick for a week or two, kills a child with PEM within
two or three days.

Health Effects of Protein:

Heart Disease:
-A high-protein diet may contribute to the progression of heart disease, foods rich in animal
protein also tend to be rich in saturated fats
-It is not surprising to find a correlation between animal- protein intake and heart disease.
-Substituting vegetable protein for animal protein improves blood lipids and decreases heart
disease mortality.
-Research suggests that elevated levels of the amino acid homocysteine may be an
independent risk factor for heart disease, heart attacks, and sudden death in patients with
heart disease.
- contrast to homocysteine, the amino acid arginine may help protect against heart disease by
lowering blood pressure and homocysteine levels.
-Additional research is needed to confirm the benefits of arginine.

Cancer:Population studies suggest a correlation between high intakes of animal proteins and
some types of cancer (cancer of the colon, breast, kidneys, pancreas, and prostate).

Adult Bone Loss (Osteoporosis):When protein intake is high, calcium excretion increases.
Whether excess protein depletes the bones of their chief mineral may depend upon the ratio
of calcium intake to protein intake.
-After all, bones need both protein and calcium. An ideal ratio has not been determined, but a
young woman whose intake meets recommendations for both nutrients has a calcium-to
protein ratio of more than 20 to 1 (milligrams to grams), which probably provides adequate
protection for the bones.
 Protein
Weight Control: Dietary protein may play a role in increasing body weight.
-Protein- rich foods are often fat-rich foods that contribute to weight gain with its
accompanying health risks.,
-weight-loss regimens that encourage a high-protein, low- carbohydrate diet may be
temporarily effective, but only because they are low-kcalorie diets.
-Selecting too many protein-rich foods, such as meat and milk, may crowd out fruits,
vegetables, and whole grains, making the diet inadequate in other nutrients.

Kidney Disease: Excretion of the end products of protein metabolism depends, in part on an
adequate fluid intake and healthy kidneys.
-A high protein intake increases the work of the kidneys.
-Restricting dietary protein, may help to slow the progression of kidney disease and limit the
formation of kidney stones in people who have these conditions.

Recommended Intakes of Protein:

-The body continuously breaks down and loses some protein and cannot store amino acids.
-To replace protein, the body needs dietary protein for two reasons.
-10 to 35 % protein. n In a 2000-kcalorie diet, that represents 200 to 700 kcalories from
protein, or 50 to 175 grams.
1. food protein is the only source of the essential amino acids,
2. it is the only practical source of nitrogen with which to build the nonessential amino acids
and other nitrogen- containing compounds the body needs.
10 to 35 % protein. In a 2000-kcalorie diet, that represents 200 to 700 kcalories
from protein, or 50 to 175 grams

Protein RDA:for adults is 0.8 grams per kg of healthy body weight per day. For infants and
children, the RDA is slightly higher.
-The RDA generously covers the needs for replacing worn-out tissue, so it increases for larger
people; it also covers the needs for building new tissue during growth, so it increases for
infants, children, and pregnant women.
-The protein RDA is the same for athletes as for others, although some fitness authorities
recommend a slightly higher intake.
Protein in Abundance:
-Most people receive more protein than they need. Even athletes in training typically don’t
need to increase their protein intakes because the additional foods they eat to meet their high
energy needs deliver protein as well.
-A single ounce of meat (or 1/2 cup legumes) delivers about 7 grams of protein, so 8 ounces of
meat alone supplies more than the RDA for an average- size person.-A cup of milk provides 8
grams of protein.
 Protein
Protein and Amino Acid Supplements:Websites,health-food stores, and popular magazine
articles advertise a wide variety of protein supplements, and people take these supplements
for many different reasons.
-They are not magic solutions , they may be harmful.
-Athletes take protein powders to build muscle.
-Dieters take them to spare their bodies’ protein while losing weight.
-Women take them to strengthen their fingernails.
-People take individual amino acids, too—to cure herpes, to make themselves sleep better, to
lose weight, and to relieve pain and depression.
-They are not magic solutions , they may be harmful.

Protein Powders: Because the body builds muscle protein from amino acids, many athletes
take protein powders with the false hope of stimulating muscle growth.
-Muscle work builds muscle; protein supplements do not, and athletes do not need them.
-Taking protein supplements does not improve athletic performance.
-Protein powders can supply amino acids to the body, but nature’s protein sources—lean
meat, milk, eggs, and legumes—supply all these amino acids and more.

Amino Acid Supplements: Single amino acids do not occur naturally in foods and offer no
benefit to the body; in fact, they may be harmful.
-The body was not designed to handle the high concentrations and unusual combinations of
amino acids found in supplements.
-An excess of one amino acid can create such a demand for a carrier that it limits the
absorption of another amino acid, presenting the possibility of a deficiency.
- Those amino acids winning the competition enter in excess, creating the possibility of
toxicity. Toxicity of single amino acids in animal studies raises concerns about their use in
human beings.
-Large doses of branched-chain amino acids can raise plasma ammonia concentrations, which
can be toxic to the brain.
-Branched-chain amino acid supplements may be useful in conditions‫ﺳﺘﻤﺮ‬ such as advanced liver
failure, but otherwise, they are not routinely recommended.
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