Republic of the Philippines

OUR LADY OF LOURDES COLLEGE FOUNDATION

COLLEGE OF MEDICAL LABORATORY SCIENCE
Vinzons Ave., Daet, Camarines Norte

PROTIEN
TABLE OF CONTENTS
I. PROTIEN
II. PROTIEN STRUTURE
 Amino group
1. Nonessential amino acids
2. Essential amino acids
 Four different structural level of protein
1. Primary Structure
2. Secondary Structure
3. Tertiary Structure
4. Quaternary Structure
III. PROTIEN FUNCTION
 Structure
 Enzyme
 Hormones
 Fluid and acid-based balance
 Transport
 Defense/Immunity
IV. PROTIEN IN DIETARY FOOD
 How much dietary protein does a person need
 Protein in food
1. Animal Sources
2. Plant Sources
 Protein Quality
V. PROTEIN DIGESTION
 Protein Digestion
1. Protein digestion by mouth
 Republic of the Philippines
OUR LADY OF LOURDES COLLEGE FOUNDATION
COLLEGE OF MEDICAL LABORATORY SCIENCE
Vinzons Ave., Daet, Camarines Norte

2. Protein digestion by stomach

3. Protein digestion in the small intestine
 What happens to the absorbed amino acids
VI. HEALTH CONSENQUENCE OF TOO LITTLE AND TOO MUCH DIETARY
PROTIEN
 Too little dietary protein
1. Kwashiorkor
2. Marasmus
 Too much dietary protein

I. PROTEIN
 Proteins are the most abundant organic molecules of the living system. They
occur in every part of the cell and constitute about 50% of the cellular dry weight.
Proteins form the fundamental basis of structure and function of life.
 The term protein is derived from a Greek word proteios, meaning holding the first
place.
II. PROTEIN STRUCTURE
 Proteins are macromolecules composed of amino acids. For this reason, amino
acids are commonly called the building blocks of Protein.
 Proteins are the only macronutrient that also contain nitrogen as part of their core
structure. In each amino acid, the elements are arranged into a specific
conformation, consisting of a central carbon bound to the following four
components:
 A hydrogen
 A nitrogen-containing amino group
 A carboxylic acid group (hence the name “amino acid”)
 A side chain

 AMINO GROUP
 Amino acid side chains vary in their size and can be as simple as one hydrogen
(glycine) or as complex as multiple carbon rings (tryptophan).
 Republic of the Philippines
OUR LADY OF LOURDES COLLEGE FOUNDATION
COLLEGE OF MEDICAL LABORATORY SCIENCE
Vinzons Ave., Daet, Camarines Norte

 They also differ in their chemical properties, thus impacting the way amino acids
act in their environment and with other molecules.
 Because of their side chains, some amino acids are polar, making them
hydrophilic and water-soluble, whereas others are nonpolar, making them
hydrophobic or water-repelling. Some amino acids carry a negative charge and
are acidic, while others carry a positive charge and are basic. Some carry no
charge.
 Nonessential amino acids are not required in the diet, because the body can
synthesize them. They’re still vital to protein synthesis, and they’re still present in
food, but because the body can make them, we don’t have to worry about
nutritional requirements.
 Essential amino acids can’t be synthesized by the body in sufficient amounts, so
they must be obtained in the diet.
 PROTIEN STRUCTURE
 Primary structure – This is the one-dimensional polypeptide chain of amino acids,
held together by peptide bonds.
 Secondary structure – The polypeptide chain folds into simple coils (also called
helices) and sheets, determined by the chemical interactions between amino
acids.
 Tertiary structure – This is the unique three-dimensional shape of a protein,
formed as the different side chains of amino acids chemically interact, either
repelling or attracting each other.
 Quaternary structure – In some proteins, multiple folded polypeptides called
subunits combine to make one larger functional protein. This is called quaternary
protein structure

III. PROTIEN FUNCTION

 Structure (Actin, myosin, collagen, elastin, keratin) Give tissues (bone, tendons,
ligaments, cartilage, skin, muscles) strength and structure
 Enzymes (Amylase, lipase, pepsin, lactase) Digest macronutrients into smaller
monomers that can be absorbed; performs steps in metabolic pathways to allow
for nutrient utilization
 Hormones (Insulin, glucagon, thyroxine) Chemical messengers that travel in
blood and coordinate processes around the body
 Fluid and acid-base balance (Albumin, hemoglobin) Maintains appropriate
balance of fluids and pH in different body compartments
 Republic of the Philippines
OUR LADY OF LOURDES COLLEGE FOUNDATION
COLLEGE OF MEDICAL LABORATORY SCIENCE
Vinzons Ave., Daet, Camarines Norte

 Transport Hemoglobin, albumin,protein channels, carrier proteinsCarry

substances around the body in the blood or lymph; help molecules cross cell
membranes
 Defense Collagen, lysozyme, antibodies Protect the body from foreign pathogens
IV. PROTEIN IN DIETARY FOOD
 The Recommended Dietary Allowance (RDA) for a sedentary adult is 0.8 g per
kg body weight per day.
 A Tolerable Upper Intake Limit for protein has not been set, but it is
recommended that you not exceed it. Protein needs are higher for the following
populations:
 growing children and adolescents
 women who are pregnant (they’re using protein to help grow a fetus)
 lactating women (breast milk has protein in it for the baby’s nutrition, so mothers
need more protein to synthesize that milk)
 athletes
 Dietary Sources of Protein Although meat is the typical food that comes to mind
when thinking of protein, many other foods are rich in protein as well, including
dairy products, eggs, beans, whole grains, and nuts.
 PROTEIN QUALITY
 High-quality complete proteins contain all nine essential amino acids.
 Lower-quality incomplete proteins do not contain all nine essential amino acids in
proportions needed to support growth and health.
V. PROTEIN DIGESTION
 Protein digestion in the mouth Unless you are eating it raw, the first step in
digesting an egg (or any other solid food) is chewing. The teeth begin the
mechanical breakdown of large egg pieces into smaller pieces that can be
swallowed. The salivary glands secrete saliva to aid swallowing and the passage
of the partially mashed egg through the esophagus.
 Protein digestion in the stomach. The mashed egg pieces enter the stomach
from the esophagus. As illustrated in the image below, both mechanical and
chemical digestion take place in the stomach. The stomach releases gastric
juices containing hydrochloric acid and the enzyme, pepsin, which initiates the
chemical digestion of protein. Muscular contractions, called peristalsis, also aid in
digestion. The powerful stomach contractions churn the partially digested protein
into a more uniform mixture, which is called chyme.
 Republic of the Philippines
OUR LADY OF LOURDES COLLEGE FOUNDATION
COLLEGE OF MEDICAL LABORATORY SCIENCE
Vinzons Ave., Daet, Camarines Norte

 Protein digestion and absorption in the small intestine The chyme leaves the
stomach and enters the small intestine, where the majority of protein digestion
occurs. The pancreas secretes digestive juices into the small intestine, and these
contain more enzymes to further break down polypeptides. The two major
pancreatic enzymes that digest proteins in the small intestine are chymotrypsin
and trypsin. Trypsin activates other protein-digesting enzymes called proteases,
and together, these enzymes break proteins down to tripeptides, dipeptides, and
individual amino acids. Tripeptides, dipeptides, and single amino acids enter the
enterocytes of the small intestine using active transport systems, which require
ATP. Once inside, the tripeptides and dipeptides are all broken down to single
amino acids, which are absorbed into the bloodstream.
 WHAT HAPPENS TO THE ABSORBED AMINO ACID
 Once the amino acids are in the blood, they are transported to the liver. As
with other macronutrients, the liver is the checkpoint for amino acid
distribution and any further breakdown of amino acids.
 Assuming the body has enough glucose and other sources of energy,
those amino acids will be used in one of the following ways:
 Protein synthesis in cells around the body
 Making nonessential amino acids needed for protein synthesis
 Making other nitrogen-containing compounds
 Rearranged and stored as fat (there is no storage form of protein)
 If there is not enough glucose or energy available, amino acids can also
be used in one of these ways:
 Rearranged into glucose for fuel for the brain and red blood cells
 Metabolized as fuel, for an immediate source of ATP
VI. HEALTH CONSENQUENCE OF TOO LITTLE AND TOO MUCH DIETARY
PROTIEN
 TOO LITTLE DIETARY PROTEIN
 Kwashiorkor is characterized by swelling (edema) of the feet and abdomen, poor
skin health, poor growth, low muscle mass, and liver malfunction. Recall that one
of the roles of protein in the body is fluid balance. Diets extremely low in protein
do not provide enough amino acids for the synthesis of the protein albumin. One
of the functions of albumin is to hold water in the blood vessels, so having lower
concentrations of blood albumin results in water moving out of the blood vessels
and into tissues, causing swelling.
 Marasmus are protein deficient, but at the same time, they’re also not taking in
enough calories. Body weights of children with Marasmus may be up to 80
 Republic of the Philippines
OUR LADY OF LOURDES COLLEGE FOUNDATION
COLLEGE OF MEDICAL LABORATORY SCIENCE
Vinzons Ave., Daet, Camarines Norte

percent less than that of a healthy child of the same age. It is characterized by an
extreme emaciated appearance, poor skin health, poor growth, and increased
risk of infection.
 TOO MUCH DIETARY PROTEIN
 There’s little evidence that a high protein diet is inherently harmful, so long as the
protein doesn’t come packaged with a lot of saturated fat and red meat
consumption is limited.

Presented and prepared by:

AGAM GLADYS KHEY S.

MR. LAWRENCE R. SANTIAGO, RMT

Instructor