General features of Amino Acids: 3.

Ornithine is similar to Lysine with an amino

group at the end of its chain.
 Contain 2 characteristic functional groups :
amino group and carboxylic acid group.  important player in the urea cycle

 amino acids used in proteins, these are  precursor to arginine and to certain
attached to a central carbon atom, Cα or α- polyamines such as spermidine and
carbon, to which are also attached a H atom spermine.
and organic side chain group R.
4. Citrulline – is derived from carbamoylation of
Amino acids ornithine on the side chain.

 Characteristically isolated as a white  it is important in the urea cycle.

crystalline ionic solids with high melting
5. Homocysteine – is an intermediate in the
point and poor solubility in organic solvents
catabolism of methionine and it is closely connected
( they are moderately soluble in water
to the functioning of the methyl
Metabolic Classification of Amino Acids – donor compound, S – adenosylmethionine

1. Glucogenic 6. У-Aminobutyric acid ( GABA ) – is an important

nuerochemical that inhibits neuronal action by
2. Ketogenic
binding to specific receptors ( GABA receptors ),
3. Glucogenic and ketogenic groups both pre and post synaptically.

1. Glucogenic amino acids – common amino acids Gabapentin – analog of GABA and use to relieve
that form pyruvate or citric acid cycle intermediates pain.
such as α ketoglutarate succinyl CoA, fumarate and
7. Dihydroxyphenylalanine ( DOPA ) – is a
oxaloactate.
precursor for the biosynthesis of amino acids such
Example : glycine, alanine,serine, cysteine, dopamine, norepinephrine, and epinephrine. It is
glutamine, proline, histidine, methionine,valine, formed by tyrosine.
isleucine
8. Histamine ( synthesized from Histidine )- is a
2. Ketogenic amino acids – amino acids that form mediator of allergic reactions.
acetyl Co-A that is converted to ketone bodies.
9. Cycloserine – a derivative of serine is an
Leucine and lysine only.
antituberculous.
3. Both glucogenic and ketogenic amino acids –
10. Azaserine inhibits reactions where amide group
Form acetyl CoA and pyruvate or citric acid cycle groups are added and acts as an anticancer drug.
intermediates. Example : phenylalanine, tyrosine,
Reactions and Separations of Amino Acids &
tryptophan, isoleucine, and arginine.
Synthesis:
Some important but less Common amino acids;
 The reaction of amino acids determined by:
1. Hydroxyproline and hydroxylysine
1. Carboxyl
 found in connective tissue protein collagen
2. α – amino and functional groups of side
2. Selenocysteine appears in few proteins such as chains.
gluthatione peroxidase.
  Reactions of both amino and carboxyl 2. Production of Serotonin from tryptophan
group
Serotonin
Amphoteric Property:
 A monoamine substance that is formed
Amino acids in solution shows amphoteric property from tryptophan and found in many animal
with the solution tissues, including the intestine and central
nervous system. In the brain, serotonin acts
 α – carboxyl group is dissociated and
as a neurotransmitter that is involved in the
negatively charge and α – amino group is
control of pain perception, the sleep-wake
protonated and positively charge
cycle, and mood. Serotonin is also produced
Reactions of carboxyl Group in some bacteria and plants.

Decarboxylation ( formation of amines ) Biosynthesis of the Nutritionally Nonessential

Amino Acids
Reaction : Decarboxylation of carboxyl group amino
acids results in the formation of amines. The  Humans can synthesize 12 of the 20
reaction is catalyzed by the enzyme decarboxylase. common amino acids from the amphibolic
1. Formation of your Histamine from histidine intermediates of glycolysis and of the citric
acid cycle
 Histamine -found in plant and animal tissue
and released from mast cells as part of an  NUTRITIONALLY NONESSENTIAL AMINO
allergic reaction in humans. It stimulates ACIDS HAVE SHORT BIOSYNTHETIC
gastric secretion and causes dilation of PATHWAYS
capillaries, constriction of bronchial smooth
Biomedical importance of amino acids:
muscle, and decreased blood pressure.
1. Inborn Errors of Amino acid metabolism
Dopamine is neurotransmitter in the brain that
plays vital roles in a variety of different behaviors.  PKU results from a defect in the enzyme
The major behaviors dopamine affects are Phenylalanine Hydroxylase (PAH), such
movement, cognition, pleasure, and motivation. that Phe is not converted to Tyrosine.

Epinephrine - A hormone secreted by the adrenal  The alternative conversion of Phe to PPA
medulla that is released into the bloodstream in causes accumulation of the latter as a toxin
response to physical or mental stress, as from fear in the Central Nervous System, which can
or injury. It initiates many bodily responses, lead to severe mental retardation.
including the stimulation of heart action and an
2. Cystinuria is an autosomal-recessive defect in
increase in blood pressure, metabolic rate, and
reabsorptive transport of cystine and the dibasic
blood glucose concentration. Also called adrenaline.
amino acids ornithine, arginine, and lysine from the
luminal fluid of the renal proximal tubule and small
intestine.

 The only phenotypic manifestation of

cystinuria is cystine urolithiasis, which often
recurs throughout an affected individual’s
lifetime. Surgical intervention is necessary,
but the cornerstones of treatment are
 dietary and medical prevention of recurrent leucine, isoleucine, and valine. Persons with
stone formation this condition must remain on this diet
permanently.
3. Alkaptonuria (black urine disease or
alcaptonuria) is a rare inherited genetic disorder of Proteins- the word protein is derived from the Gk.
phenylalanine and tyrosine metabolism. word “ proteios” means primary.

 Commonly recommended treatments  Out of the total body weight of humans

include large doses of ascorbic acid (vitamin 3/4ths are made up proteins.
C)and dietary restriction of phenylalanine
 Content of proteins: Carbon, Hydrogen,
and tyrosine.
Oxygen and Nitrogen
4. Tyrosinemia

 a genetic disorder characterized by

elevated blood levels of the amino acid
tyrosine, a building block of most proteins.

 caused by the shortage (deficiency) of one

of the enzymes required for the multistep
process that breaks down tyrosine. If
untreated, tyrosine and its byproducts build
up in tissues and organs, which leads to
serious medical problems.

5. Maple Syrup Urine Disease

an inherited disorder in which the body is unable to

process certain protein building blocks (amino
acids) properly. The condition gets its name from
the distinctive sweet odor of affected infants' urine.
Beginning in early infancy, this condition is
characterized by poor feeding, vomiting, lack of
energy (lethargy), and developmental delay. If
untreated, maple syrup urine disease can lead to
seizures, coma, and death.
Amino acids and Peptide Linkages
Treatment
 in proteins amino acids are joined by
 When the condition is diagnosed, and
peptide bonds
during episodes, treatment involves eating
a protein-free diet. Fluids, sugars, and  String of amino acids are joined together by
possibly fats are given through a vein (IV). peptide bonds is called polypeptide
Peritoneal dialysis or hemodialysis can be
 oligopeptide for shorter chain.
used to reduce the level of amino acids.
 Peptide bonds are amide linkages formed
 Long term treatment requires a special
by condensation of the α-carboxyl group of
diet. The diet includes a man-made infant
formula with low levels of the amino acids
 one amino acid with α amino of another  regular spatial arrangement of the atoms
amino acid along the chain backbone.

Protein Classification:  stabilized by weak, noncovalent

interactions such as hydrogen bond,
1. Globular Proteins
hydrophobic interactions, and electrostatic
2. Fibrous proteins attractions.

Two Principal secondary structures;

1. α-Helix

2. Β-Helix

General biological functions of Proteins

1. Mechanical support and cushioning:

collagen, elastin

2. Mechanical work: actin, myosin,tubulin

3. Catalysis: enzymes ribonuclease,

hexokinases, DNA polymerases

4. Transport and storage: hemoglobin,

myoglobin, serum albumin

5. Communication and defense: antibodies,

peptide hormone, hormone and
neurotransmitters receptors  These turns may flexible loops of a new
amino acids, serving to join different
1. Secondary and Higher-order structures:
stretches of secondary structure, or they
 The primary structure of a macromolecule may be sharp turns the reverse the chain
such as protein or nucleic acid refers to the direction.
sequence of covalently bonded residues
Tertiary Structure
along the main chain.
 The tertiary of a macromolecule refers to a
 Polypeptide chains determines its primary
large scale organization of the polymer
structure
chain than is seen at the level of the
 Secondary structure - next higher level of secondary structure.
macromolecular structure.
 arrangement includes elements of
secondary and packed against each other.
  stabilized by non-covalent interaction  large protein may contain 2 or more
regions of the polypeptide chain that
 covalent linkages- disulfide bonds between
individually have a compact folded called
the cysteine residues.
Domain.
 fibrous and globular can be distinguished
Example:
by their tertiary structures and chemical
properties. 1. Troponin C α helices

Fibrous proteins 2. Calmodulin α helices Ca ion binding

domains
 tend to extend tertiary conformations
3. Nicotinamide binding site in glyceradehyde-
 roles in mechanical support and flexibility
3-phosphate dehydrogenase
Important fibrous protein is Collagen
4. Immunoglobulins folds in immunoglobulin
 subtypes of collagen found in different G.
connective tissue and skin structure.
Quaternary Structure
 it has high proportion of Glycine, Alanine
 multisubunit structure
and Hydroxyproline residues in its
polypeptide chains  association of protein chains with nucleic
acids as in ribosomes and nucleosomes
Keratin
 identical or non identical polypeptide chain
 mostly found in hairs, nails, and claws also
stiffens and support the skin  simplest form is dimer

 secondary and tertiary structures  hemoglobin – tetramer composed of α and

contributes directly to the necessary β subunits
mechanical properties for these uses.
 Glyceraldehyde-3-phosphate
 high proportion of keratin structure is dehydrogenase – tetramer
called the coiled coil.
 Glutamine synthetase
Globular Proteins
Classification of proteins base on Composition and
 spherical in shape solubility

 surface – relatively rough, not smooth, with 1. Simple Proteins

ridges and valleys , some of which it maybe
2. Conjugated protein
quite deep.
1. Simple Protein
 Mostly the amino acid found in surfaces is
non polar  Contain only amino acids
 polar and ionic side chains help to solvate I. Albumins
the protein
 Soluble in water
 non polar - hydrophobic
 Coagulated by heat
Example: V. Lectins

 Human serum albumin MW – 69,000  precipitated by 30 – 60% ammonium

sulfate
 Lactalbumin of milk
 high affinity with sugar groups
 Egg albumin
Example:
 Albumin is clinically used in the treatment
of severe hypoalbuminemia and as a plasma A. lectin from Dolichus biflorus with
expander. agglutinate human blood group A1 RBCs.

 Lactalbumin nhances efficiency of brain B. Phytohemagglutinin a lectin of from

function. ( cow’s milk ) Phaseolus vulgaris agglutinates RBCs and
WBCs.
II. Globulins
C. Concanavalin-A from legumes will attach to
 insoluble in pure water
mannose and glucose
 soluble in salt solns.
VI. Scleroproteins
 coagulated by heat
 insoluble in water, salt solns and organic
Examples: egg globulin, serum globulins, legumin solvents
peas
 soluble in hot strong acids (sulfuric,
III. Protamines hydrochloric, nitric, and phosphoric. )

 soluble in water, dilute acids and alkalies  form supporting tissues

 not coagulated by heat Example: collagen in bones, cartilage and tendon,

keratin hair, horn,nail and hoof.
 contain large numbers of arginine and
lysine residues and are strongly basic 2. Conjugated Proteins

 combine with other acidic proteins  Combinations of protein with a non-protein

part called prosthetic group.
Example : Protamine zinc insulate is a common
commercial preparation of insulin.

IV. Prolamines

 soluble in 70 – 80% alcohol

 insoluble in pure water

 Rich in proline but lack lysine

Example : cazein in corn, gliadin in wheat,hordein in

barley
Example of protein drugs:  Avoid confrontation and requests that
might lead to frustration

 Remain calm and supportive if the patient

becomes upset

 Maintain a consistent environment

 Provide frequent cues and reminders to

reorient the patient

 Adjust expectations for the patient as he or

Protein Diseases
she declines in capacity.
1. Alzheimer Disease
Sickle cell anemia ( drepanocytosis )
 formation of amyloid protein which is
 genetic homozygous , recessive
insoluble that causes plaques in the
neuronal cells.  disorder of blood caused by a single
nucleotide alteration in the gene for B-
 consist of Beta – pleated proteins
globin
 protein mis-folding
 production of abnormal type of
Primary Nursing Diagnosis hemoglobin (HBs)

 Self-care deficit related to impaired  HBs become insoluble when the blood is
cognitive and motor function deprived of oxygen and precipitates forming
elongated that distort the blood into
 Outcomes. Self-care: Activities of daily living
characteristic sickle shape.
—Bathing, Hygiene, Eating,
Toileting; Cognitive ability; Comfort level; Symptoms of sickle cell anemia vary and are only
Role performance; Social interaction skills; somewhat based on the amount of HbS.
Hope
 Anemia. Anemia is always present; usually,
 Interventions. Self-care assistance: Bathing hemoglobin values are 7 to 10g/dl.
and Hygiene; Oral health
 Jaundice. Jaundice is characteristic and
management; Behavior management;
usually obvious in the sclerae.
Body image enhancement; Emotional
support; Mutual goal setting; Exercise  Dysrhythmias. Dysrhythmias and heart
therapy; Discharge planning failure may occur in adults.
The initial management of the patient begins  Enlargement of the bones. The bone
with education of the family and caregivers marrow expands in childhood in a
regarding the disease, the prognosis, and compensatory effort to offset anemia,
changes in lifestyle that are necessary as the sometimes leading to enlargement of the
disease progresses. bones of the face and skull
 Basic collaborative principles include:

 Keep requests for the patient simple

Nursing Managing Pain Initial Management

 Use patient’s subjective description of pain  Early clinical recognition of

and pain rating on a pain scale to guide the methemoglobinemia is paramount, as
use of analgesic agents. patients often have only vague, nonspecific
complaints, especially in the initial phase.
 Support and elevate any joint that is acutely
High levels of methemoglobinemia can be
swollen until swelling diminishes.
life-threatening and necessitate emergency
 Teach patient relaxation techniques, therapy.
breathing exercises, and distraction to ease
 Patients with chronic mild increases in
pain.
methemoglobin level may be completely
 When acute painful episode has diminished, asymptomatic and require no specific
implement aggressive measures to preserve therapy (provided that they have no
function. evidence of end-organ damage)

Methemoglobinemias Once the diagnosis of methemoglobinemia has

been confirmed and appropriate management has
 oxidation of the heme component to Ferric been initiated, the underlying etiology should be
form which cannot bind oxygen, sought.
 certain mutations in the α and β – globin In acquired methemoglobinemia, if the toxin or
chain. drug is not known from the history, it may be
 Deficiency of NADH – cytochrome identified by obtaining blood levels, performing
b5reductase responsible for the conversion gastric lavage, or both.
of methemoglobin to haemoglobin In asymptomatic patients with low levels of
characterized by chocolate cyanosis. methemoglobin, monitoring serial serum levels may
 brownish blue coloration of the skin and be all that is necessary. The levels normalize over
mucous membrane and chocolate colored time unless recurrent or chronic exposure to the
blood offending agent occurs.

Hyperbaric oxygen  treatment is another option for

situations where methylene blue therapy is
ineffective or contraindicated. This approach
permits tissue oxygenation to occur through oxygen
dissolved in plasma, rather than through
hemoglobin-bound oxygen.

Infants with methemoglobinemia due to metabolic

acidosis should be treated with IV hydration and
bicarbonate to reverse the acidosis. The NADPH-
dependent methemoglobin reductase enzyme
system requires glucose for the clearance of
methemoglobin. Therefore, IV hydration with
dextrose 5% in water (D5W) is often effective.

GOD BLESS! YOU