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Biochem Protein Module 3.1

The document provides information about a pre-learning activity and pre-test examination for a biochemistry module focusing on proteins for a nursing course at St. Paul College of Ilocos Sur. The pre-test examines students' understanding of the biological significance and specific functions of proteins, including their roles in providing structural framework, maintaining osmotic integrity, acting as enzymes, hormones, carriers of oxygen and lipids, antibody formation, and acting as buffers. It also contains multiple choice questions testing students' knowledge of protein hydrolysis, classification of protoamines, amino acid groups and properties, examples of primary proteins, diseases associated with proteins during pregnancy, childhood protein deficiency disorders, and amino acid color tests. The instructor is listed as Mel
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0% found this document useful (0 votes)
92 views23 pages

Biochem Protein Module 3.1

The document provides information about a pre-learning activity and pre-test examination for a biochemistry module focusing on proteins for a nursing course at St. Paul College of Ilocos Sur. The pre-test examines students' understanding of the biological significance and specific functions of proteins, including their roles in providing structural framework, maintaining osmotic integrity, acting as enzymes, hormones, carriers of oxygen and lipids, antibody formation, and acting as buffers. It also contains multiple choice questions testing students' knowledge of protein hydrolysis, classification of protoamines, amino acid groups and properties, examples of primary proteins, diseases associated with proteins during pregnancy, childhood protein deficiency disorders, and amino acid color tests. The instructor is listed as Mel
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as DOCX, PDF, TXT or read online on Scribd
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St.

Paul College of Ilocos Sur


St. Paul Avenue, 2727, Bantay, Ilocos Sur

NSC 101- BIOCHEMISTRY

Module 3
(Proteins)

Melanio P. Rojas Jr
Clinical Instructor
St. Paul College of Ilocos Sur
(Member, St. Paul University System)
St. Paul Avenue 2727, Bantay, Ilocos Sur

DEPARTMENT OF NURSING

PRE-LEARNING ACTIVITY

PRE-TEST EXAMINATION: MODULE 3

NCM 104: Community Health Nursing I- Individual and Families as Clients


First Semester A.Y. 2019-2020
(Lecture)

Melanio P. Rojas Jr. MAN


(Clinical Instructor)

Name: _______________________________ Score: ___________________


Course/Year: __________________________ Date: ____________________

I. Explain the specific functions of the difference biological significance in protein.


Biological Significance Specific Functions
1. Providing the structural framework of Like all other cellular membranes, the plasma
tissues, membranes and cells walls membrane consists of both lipids and proteins.
The fundamental structure of the membrane is
the phospholipid bilayer, which forms a stable
barrier between two aqueous compartments. In
the case of the plasma membrane, these
compartments are the inside and the outside of
the cell. Proteins embedded within the
phospholipid bilayer carry out the specific
functions of the plasma membrane, including
selective transport of molecules and cell-cell
recognition.

2. Maintain osmotic integrity Osmosis is the diffusion of water across a


membrane in response to osmotic
pressure caused by an imbalance of molecules on
either side of the membrane. Osmoregulation is
the process of maintenance of salt and water
balance ( osmotic balance) across membranes
within the body’s fluids, which are composed of
water, plus electrolytes and non-electrolytes.
An electrolyte is a solute that dissociates into
ions when dissolved in water.
3. Storage of some particular element

4. Enzymes, to catalyze biological reactions Enzymes are biological molecules (typically


proteins) that significantly speed up the rate of
virtually all of the chemical reactions that take
place within cells.
Enzymes are highly selective catalysts, meaning
that each enzyme only speeds up a specific
reaction.

5. Hormone regulate metabolic process GH functions as a major metabolic hormone in


the adult by optimizing body composition and
physical function as well as regulating energy and
substrate metabolism. Metabolic actions of GH
also closely interact with those of insulin in the
control of fat, glucose, and
protein metabolism during fasted and fed states.

6. Carriage of molecular oxygen The transport of oxygen in blood is undertaken


by hemoglobin, the largest component of red
blood cells. This protein collects oxygen in
respiratory organs, mainly in the lungs, and
releases it in tissues in order to generate the
energy necessary for cell survival.

7. Transportation of lipids Lipids perform three primary biological functions


within the body: they serve as structural
components of cell membranes, function
as energy storehouses, and function as important
signaling molecules.
8. Taking part in antibody formation Antibody, also called immunoglobulin, a
protective protein produced by the immune
system in response to the presence of a foreign
substance, called an antigen. Antibodies
recognize and latch onto antigens in order to
remove them from the body. A wide range of
substances are regarded by the body as antigens,
including disease-causing organisms and toxic
materials such as insect venom.

9. Acting to a certain as buffers in biological A buffer is a chemical substance that helps


process maintain a relatively constant pH in a solution,
even in the face of addition of acids or
bases. Buffering is important in living systems as
a means of maintaining a fairly constant internal
environment, also known as homeostasis.
St. Paul College of Ilocos Sur
(Member, St. Paul University System)
St. Paul Avenue 2727, Bantay, Ilocos Sur

DEPARTMENT OF NURSING

PRE-LEARNING ACTIVITY

PRE-TEST EXAMINATION: MODULE 3

NCM 104: Community Health Nursing I- Individual and Families as Clients


First Semester A.Y. 2019-2020
(Lecture)

Melanio P. Rojas Jr. MAN


(Clinical Instructor)

Name: _______________________________ Score: ___________________


Course/Year: __________________________ Date: ____________________

MULTIPLE CHOICE: Choose the best answer place your answer on the answer sheet provided.
Shade the box that correspond the letter of your choice. Use black ink ball
pen only. ERASURES MEAN WRONG.

1. Proteins can hydrolyzed, which of the following? Select all that apply.

A. Picric acid C. 25% H₂S04


B. KOH D. Glutelins

2. Protoamines characterized by: Select all that apply.


A. Insoluble in ammonia
B. Soluble in water
C. Stable salts with strong minerals
D. Coagulated on heating
3. Which of the following group of amino acids?

A. Lysine C. Proline
B. Leucine D. Arginine

4. Which of the following is true regarding physical properties of amino acid?


A. Amino acids can be methylated
B. Amino acids can react with nitrous acid
C. Amino acids appear as crystalline
D. Amino acids form esters
5. The following is an example of primary protein except?

A. Peptides C. Peptones
B. Edestin D. Phosphotungstic acid

6. Which color is commonly produce on skin which has come in contact with nitric acid?

A. Green C. Blue
B. Yellow D. Red
7. Which diseases is associated in protein during pregnancy?
A. Eclampsia
B. Preeclampsia
C. Pregnancy Induced Hypertension
D. Gestational Diabetes

8. Which childhood disorder that causes protein deficiency?

A. Marasmus C. Meningitis
B. Kwashiorkor D. Beri-Beri

9. Which of the following test that give reactions of amino acid into color pink?

A. Sakaguchi test D. Xanthroproteic reaction


B. Reduced sulfur test E. Tryptopohan reaction
C. Bromine-water reaction

10. Amino acids may be determined by except:

A. Colorimetric methods C. Folin amino acid methods


B. Biological methods D. Chromatopgraphic analysis

11. All but one is true regarding sakaguchi test?


A. This test is consist of 5 ml of a 2 percent solution of protein
B. The half procedure mixture is treated with 0.3 N sodium hypochorite
C. Only compounds containing the free guanidine group react
D. Accordingly the color test is specific for cystine
12. The formation of urea from ammonia is represented by the overall equation?
A. 2NH₂+CO₂-------------NH₂-CONH₂+H₂0
B. 2NH₃+CO₂-------------NH₂-CONH₂+H₂0
C. 2NH₃+CO₂-------------NH₂-CONH₃+H²0
D. 2NH₃+CO₂-------------NH₂-CONH₂+H²0
13. It plays catalytic role in the synthesis of urea via the ornithine cycle is called______.

A. Proline C. Arginine
B. Alanine D. Threonine

14. Which of the following is antidote for metallic poisoning except?

A. Egg white C. Baking soda


B. Milk D. Liquid protein

15. This is protein structure that causes the chain to twist into a coil or a helix or pleated-like chain of
amino acids is called__________.

A. Secondary protein structure C. Tertiary protein structure


B. Primary protein structure D. None of the above

16. Which of the following is considered a chemical agents?

A. Heavy metals C. Mechanical agitation


B. Surface action D. High pressure

17. Which organ that catalyzes the decarboxylation of histidine and histamine which is an active
stimulant of gastric secretion except?

A. Pancreas B. Liver
C. Kidneys D. Intestines

18. Which amino acids that is consider as hydrophilic?

A. Alanine C. Cysteine
B. Valine D. Serine

19. This is the most delicate reagent for detecting presence of protein of an alpha-amino acid except
proline and hydroxyproline is called_______.

A. Folin’s reagent C. Reduced sulfur test


B. Ninhydrin reaction D. Diacetyl test

20. Which of the following reactions are used in amino acids in the body for detoxifying purposes
except?
A. Acetylated
B. Benzylated
C. Methylated
D. Decarboxylated

Activity No. 1. Draw the structure of Amino Acids

Amino Functions Structure


Acids
Glycine  This amino acid is the first of all
necessary ones for a healthy digestive
system, because it helps regulate the
synthesis of the bile acid utilized to
help you digest fats. Glycine also plays
a role as an inhibitory
neurotransmitter in your central
nervous system, particularly in the
spinal cord, in the brainstem, and in
the retina. This amino acid is essential
for the development and quality of
human skeletal muscles, tissues, and
structural integrity, as well as for the
synthesis of nucleic acids.

 Glycine is a non-essential amino acid,


implying that our bodies are able to
produce it. Like many other amino
acids, this one is used to help create
muscle tissues and convert glucose
into energy. In addition, it is also vital
for maintaining healthy central
nervous and digestive systems. The
latest researches showed that it can
also provide protection against some
types of cancer through antioxidants.

Alanine  Alanine is basically a non-essential


amino acid sometimes found in high
levels in its free state in human
plasma. This amino acid is synthesized
by reductive amination of pyruvate,
and participates in sugar and acid
metabolism. It is also known for
increasing immunity and providing
energy for brain and central nervous
system, let alone the muscle tissue. In
addition, Alanine plays a central role in
glucose-Alanine cycle taking place
between tissues and liver.

Valine  This amino acid aids preventing the


breakdown of muscle, because it
supplies the muscles with an extra
glucose responsible for the energy
production during physical activity.
Valine is also a precursor in the
penicillin biosynthetic pathway and is
known for inhibiting the transport of
Tryptophan across the blood-brain
barrier.
 In other words, Valine is an essential
amino acid important for smooth
nervous system and cognitive
functioning. Valine is one of the three
branched-chain amino acids, along
with Leucine and Isoleucine. This
amino acid cannot be produced by
your body and must be obtained
through food or through supplements.
Valine is important for everyday body
functions and for maintaining muscles,
as well as for the regulation of the
immune system. This particular amino
acid is not processed by the liver, but is
taken up by muscles. You can obtain it
through kidney beans, leafy
vegetables, poultry and milk.

Leucine  Leucine is considered a vital amino


acid for the protein synthesis and
various metabolic functions - in other
words, it is an essential amino acid,
which helps in regulating the blood-
sugar levels, promotes the growth and
the recovery of muscle and bone
tissues, as well as the production of
the growth hormone. This amino acid
is also known for preventing the
breakdown of muscle proteins caused
by injury or stress. In addition, Leucine
may be beneficial for people suffering
from phenylketonuria.

Isoleucine
Phenylalanine  Phenylalanine is a precursor of
Tyrosine, combined with which it
leads to the formation of
adrenaline. In turn, adrenaline is
converted into a brain chemical
utilized to produce noradrenaline
responsible for promoting mental
alertness and memory, and also
for the elevation of mood and for
the suppression of appetite.
 Since noradrenaline affects mood,
various forms of phenylalanine
have been suggested to treat such
conditions as lack of energy,
memory problems, depression,
confusion, decreased alertness,
and lack of appetite, all of which
are considered to be caused by
the Phenylalanine deficiency.

Methionine  Methionine is an amino acid that


produces several important
molecules in your body. These
molecules are essential for the
proper functioning of your cells.

Cysteine  Cysteine is one of the few amino


acids that contains sulfur . This
allows cysteine to bond in a
special way and maintain the
structure of proteins in the body.
Cysteine is a component of the
antioxidant glutathione . The body
also uses cysteine to
produce taurine , another amino
acid.

Proline  Proline is an essential component


of collagen, and therefore is vital
for proper functioning of joints and
tendons. Besides, this amino acid
helps maintain and strengthen
heart muscles. Since Proline is a
non-essential amino acid, which
can be obtained from Glutamic
acid, it is not necessary to be
obtained additionally from dietary
sources. In other words, human
body is able to produce enough
Proline for its own use. Like many
other amino acids, Proline can be
easily utilized as an energy source
for the body.
Serine  Serine plays an important role in
various biosynthetic pathways. In
addition, it is the precursor to a
number of amino acids like Glycine
and Cysteine. Besides, it also helps
an enzyme catalyze its reaction -
the hydrolysis of peptide bonds in
polypeptides and proteins, which is
basically a major function in the
digestive process.
 Serine is recognized as a non-
essential amino acid obtained from
another amino acid called Glycine
and is believed to be important to
overall good health, both physical
and mental. This amino acid is
particularly essential for proper
functioning of your brain and of
your central nervous system.
 One of the Serine's functions is to
help form the phospholipids which
are necessary for creating every
cell in the human body. In addition,
this amino acid is involved in the
functioning of RNA and DNA, in the
muscle formation as well as in the
maintenance of a proper immune
system. Tryptophan, an essential
amino acid used to make serotonin
(a mood-determining brain
chemical), also cannot be produced
without Serine. Meanwhile, both
serotonin and Tryptophan
shortages are believed to cause
depression, insomnia, and anxiety.
Numerous researches suggest that
low levels of this amino acid are
responsible for the chronic fatigue
syndrome and fibromyalgia.
Threonine  Threonine is an essential amino
acid, i.e., it is vital for your health,
but it canott be synthesized by
your body and therefore has to be
obtained from a diet. This amino
acid supports central nervous,
cardiovascular, liver, and immune
system functioning - just to name a
few. Moreover, it helps in the
synthesis of glycine and serine
which, in their turn, assist in the
production of collagen, elastin, and
muscle tissue. In addition,
Threonine aids building strong
bones and tooth enamel and
speeds up a wound healing process
after trauma or surgery by
boosting up the immune system.
 Threonine works the following
way: it combines with aspartic acid
and Methionine to jointly help liver
digest fats and fatty acids. This
process helps reduce the
accumulation of fat in the liver,
which would otherwise affect the
liver function. This amino acid is
also useful in treating Lou Gehrig's
disease, aka Amyotrophic Lateral
Sclerosis. Scientific researches
show that Threonine treatment
also helps alleviate symptoms of
Multiple Sclerosis - another disease
affecting nerves and muscles.
Besides, Threonine is recognized as
an immunostimulant promoting
the growth of thymus gland.

Tyrosine  Tyrosine represents a starting


material for neurotransmitters.
This amino acid also increases
plasma neurotransmitter levels,
especially dopamine and
noradrenalin, as well as
participates in the synthesis of
enkephalins providing pain-
relieving effects in the body. The
aforementioned compounds are
very important in terms of brain
health, since they are responsible
for transmitting nerve impulses
and preventing conditions like
depression. Besides, dopamine is
also essential for the mental
functioning and mood, and
therefore is widely used to treat
mild depression and even
stimulate sex drive. According to
the numerous studies that were
carried out throughout the world,
this amino acid proved to be
efficient in alleviating stress,
anxiety and kept the patients
generally more alert.
Asparagine  Asparagine is one of the twenty
most common amino acids on our
planet - one of the principal and
the most abundant elements that
help to transport nitrogen. Besides,
this amino acid is required by
human body cells for the protein
production. It can be produced in
the liver and is recognized
worldwide for its ability to help
increase the resistance to fatigue,
thus improving athletic stamina.

Glutamine  Glutamine, also known as L-


Glutamine, seems to be the most
active amino acid involved in lots
of metabolic processes. For
example, glutamine is converted to
glucose if your body needs more
glucose as an energy source.
Besides, it also participates in
maintaining of a normal blood
glucose level and the proper pH
range. In fact, glutamine was
recognized as the most abundant
free amino acid found in the
human muscles and in plasma. A
human body utilizes this amino
acid at high rates for rapidly
dividing cells, like leucocytes, in
order to supply them with an
energy, i.e., to create the best
conditions for the nucleotide
biosynthesis. In other words,
glutamine is considered to be vital
for the proper immune function.
Aspartate  Aspartate is believed to help your
body promote a robust
metabolism. From time to time it is
used to treat depression and
fatigue. This amino acid plays a key
role in the citric acid cycle (also
known as Krebs cycle), within
which a number of other amino
acids and biochemicals are formed.

Lysine  Lysine is recognized as an amino


acid necessary as a building block
for all proteins in your body. It
plays a major role in calcium
absorption, as well as in helping
building muscle protein. Besides,
Lysine aids in recovering from
surgery or traumas and helps your
body produce hormones, enzymes,
and antibodies. This amino acid
was also proved to depress the
central nervous system while
having antiseizure properties.
 Lysine is an essential amino
acid, implying that it is
important for human health,
though our body cannot produce
it. Therefore, it has to be
obtained from food. Lysine is a
type of amino acids that are the
building blocks of proteins. It is
vital for proper growth and plays
an important role in the
production of carnitine, which is
a nutrient that transforms fatty
acids into energy and lowers
cholesterol levels. In addition,
this amino acid is proved to help
the human body absorb calcium,
while playing an essential role in
the formation of collagen - a
substance necessary for both
bones and connective tissues
like skin, cartilage, and tendon.

Histidine  Histidine is usually referred to as a


semi-essential amino acid because
it is nonessential in adults but is
essential in the diet of infants and
individuals with uremia - a kidney
disorder.
 Our body mostly needs Histidine to
regulate and to utilize essential
trace elements like iron, copper,
molybdenum, zinc, and
manganese. This amino acid is also
essential in forming numerous
metal-bearing enzymes and
compounds, such as the
antioxidant super oxide dismutase.
Glutamine  Glutamine, also known as L-
Glutamine, seems to be the most
active amino acid involved in lots
of metabolic processes. For
example, glutamine is converted to
glucose if your body needs more
glucose as an energy source.
 Besides, it also participates in
maintaining of a normal blood
glucose level and the proper pH
range. In fact, glutamine was
recognized as the most abundant
free amino acid found in the
human muscles and in plasma. A
human body utilizes this amino
acid at high rates for rapidly
dividing cells, like leucocytes, in
order to supply them with an
energy, i.e., to create the best
conditions for the nucleotide
biosynthesis. In other words,
glutamine is considered to be vital
for the proper immune function.

Aspartate  Aspartate is believed to help your


body promote a robust
metabolism. From time to time it is
used to treat depression and
fatigue. This amino acid plays a key
role in the citric acid cycle (also
known as Krebs cycle), within
which a number of other amino
acids and biochemicals are formed.

Lysine  Lysine is recognized as an amino


acid necessary as a building block
for all proteins in your body. It
plays a major role in calcium
absorption, as well as in helping
building muscle protein. Besides,
Lysine aids in recovering from
surgery or traumas and helps your
body produce hormones, enzymes,
and antibodies. This amino acid
was also proved to depress the
central nervous system while
having antiseizure properties.
 Lysine is an essential amino
acid, implying that it is
important for human health,
though our body cannot produce
it. Therefore, it has to be
obtained from food. Lysine is a
type of amino acids that are the
building blocks of proteins. It is
vital for proper growth and plays
an important role in the
production of carnitine, which is
a nutrient that transforms fatty
acids into energy and lowers
cholesterol levels. In addition,
this amino acid is proved to help
the human body absorb calcium,
while playing an essential role in
the formation of collagen - a
substance necessary for both
bones and connective tissues
like skin, cartilage, and tendon.
Activity No. 2. Draw and discuss the general pathways of protein metabolism.
Protein metabolism increases overall during pregnancy, not only in the areas where new tissue is being
formed, and plasma protein turnover in particular is markedly increased.126 The rate of protein
metabolism is higher in the placenta than in any other tissue, including the liver.126 In the first half of
pregnancy the placenta grows faster than the fetus; in the second half the situation is reversed. Protein
synthesis from both carbohydrate and amino-acid precursors is more than twice as high in human
placentae before 16 weeks as it is at term. The rate of placental protein synthesis at different stages
parallels the rates of glucose metabolism via the pentose pathway and of RNA and DNA turnover, which
are all significantly higher in the early rapidly proliferating placenta than at term. Pharmacologically
induced changes in pentose shunt activity also induce corresponding changes in nucleic acid and protein
synthesis in the placenta and other rapidly proliferating tissues. These findings suggest that the
availability of pentose sugars is a key rate-limiting factor in nucleic acid production, and hence in protein
synthesis, and also support the view that protein synthesis in the early placenta is directed primarily
towards fulfilling growth requirements while in later weeks it is directed mainly towards function. This
makes the placenta a very suitable model for studying nucleic acid formation and protein synthesis in
both replicating and differentiating cells.

Activity no. 3. Applying in Clinical Setting


Maria is a 6 year old with a diagnosis of nephrotic syndrome. Upon the assessment of
Nurse Jerich revealed that Maria gained weight, her urine is cloudy and poor appetite.
Whatis the relationship of protein regarding her condition? What will be the diet of
Maria, diagnostic test, intervention and treatmen

Nursing Care Plan- Intervention/Treatment Rationale


Definition:
1. Preventing Infection Diagnostic
Protect Tests/Procedure:
the child from anyone with an infection:
Nephrotic syndrome is a  Urine tests. A urinalysis can reveal
kidney disorder that causes your body to abnormalities in your urine, such
pass too much protein in your as large amounts of protein. ...
urine. Nephrotic syndrome is usually caused  Blood tests. A blood test can show
by damage to the clusters of small blood low levels of the protein albumin
staff, family, visitors, and other
children; handwashing and strict medical asepsis
are essential; and observe for any early signs of
infection.
2. Monitoring Fluid intake and output. Accurately monitor and document intake and
output; weigh the child at the same time every
day, on the same scale in the same clothing;
measure the child’s abdomen daily at the level of
the umbilicus.
3. Promoting energy conservation.  Bed rest is common during the edema stage of
the condition; balance the activity with rest
periods and encourage the child to rest when
fatigued; plan quiet, age-appropriate activities
that interest the child.
4. Improving nutritional intake. Offer a visually appealing and nutritious diet;
consult the child and the family to learn which
foods are appealing to the child; serving six small
meals my help increase the child’s total intake
better.
5. Promoting skin integrity. Inspect all skin surfaces regularly for breakdown;
turn and position the child every 2 hours; protect
skin surfaces from pressure by means of pillows
and padding; protect overlapping skin surfaces
from rubbing by careful placement of cotton
gauze; bathe the child regularly; a sheer dusting
of cornstarch ma be soothing to the skin.

References:
https://nurseslabs.com/nephrotic-syndrome/#:~:text=Nursing%20interventions%20for%20a
%20child,the%20level%20of%20the%20umbilicus.

https://aminoacidsguide.com/Gln.html

https://aminoacidsguide.com/Met.html

https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/protein-
metabolism

https://www.ncbi.nlm.nih.gov/books/NBK9898/

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