2.Red blood cells
Dr. Gopi Mulaka
St. Martinus University Faculty of
Medicine, Curacao
II)Red Blood Cells(Erythrocytes)
II) Blood Cells
Øred blood cells
(erythrocytes)
Øwhite blood
cells
(leucocytes)
Ø platelets
(thrombocytes).
3
4
5
Red cells (Erythrocytes)
Ø Average Number of RBCs: 5.1 to 5.8 million in males(5,200,000)
and 4.3 to 5.2 million in females(4,700,000) per milliliter blood.
Ø Shape: flat, biconcave discs, about 7 um in diameter and 2.2 um
thick.
Ø Importance of the unique shape- provides an increased surface
area through which gas can diffuse.
• The average volume of the RBC is 90 to 95 cubic micrometers. (MCV)
(The RBC is a “bag” that can be deformed into almost any shape.)
6
EM of normal red blood cells
7
MCHC(Mean corpuscular hemoglobin concentration)
Ø RBCs can concentrate hemoglobin in the cell
fluid up to about 34 grams per 100 milliliters
of cells.(34% MCHC).
Ø The % of Hb is almost always near the
maximum on each cell.
Life Span of Red Cells
ØErythrocytes lack a nucleus and mitochondria.
Ø (they get energy from anaerobic (but not aerobic) respiration).
ØLife span: about 120 days
Ødestroyed by phagocytic cells in the liver, spleen and bone marrow.
9
Physical and Chemical Properties of the Red Cells
•Hematocrit
•Function
•Material for the production
•Erythropoiesis
10
Hematocrit
ØConcept: The percentage of blood volume occupied by the
packed red blood cell volume.
ØNormal range:
1)Men 40% - 50%,
2) Women 37% - 48%
11
MEASUREMENT OF HAEMATOCRIT
The haematocrit ratio (Ht) is the proportion of blood made up of cells mainly red blood cells.
1.0
plasma
centrifuge
0.5
buffy coat
red cells
0
blood
sample
After centrifugation the
heavier red cells settle to
the bottom of the tube.
The straw-coloured plasma
remains at the top.
The two layers are
separated by a ‘buffy coat’
of white cells and platelets.
Normal values for Ht
range between 0.42 - 0.47,
generally larger in men
than women.
12
RBCs Function:
ØTo transport oxygen from the lungs to the tissue (function of
hemoglobin)
ØTo transport carbon dioxide in blood.
ØTransport of Hemoglobin.
The arterial and venous red cell
13
Acid-base
buffering
• Besides transport of
haemoglobin .....
• Transport of huge amounts of
CO2 in the form of bicarbonate
ion (HCO3−) from the tissues to
the lungs.
• Haemoglobin is an excellent acidbase buffer, and RBCs are
responsible for most of the acidbase buffering power of whole
blood.
Carbonic Anhydrase
Henderson-Hasselbalch equation
Erythropoiesis
• Concept: The production of new red
blood cells to replace the old and
died ones.
• In the adult, all the red cells are
produced in bone marrow in Axial
skeleton and Distal long bones.
16
Areas of the body that produce Red blood cells
Fetus
• Early weeks of embryonic life = yolk
sac.
• Middle trimester of gestation = Liver +
spleen + lymph nodes.
• Last month of gestation and after
birth, = Bone marrow.
Adult
• All bones until 5 years of age.
• The marrow of the long bones,
becomes fatty and produces no more
RBCs at about 20 years of age.
• Beyond 20 years = membranous
bones, (vertebrae, sternum, ribs, and
ilia).
• The remaining bone marrow becomes
less productive as age increases.
Erythropoiesis- Pluripotent stem cells in the bone marrow.
Ø It can produce any type of blood cells.
Ø All the circulating blood cells come from a single type of cell called the
Pluripotential hematopoietic stem cell(PHSC).
Ø When they divide, some cells stay in the bone marrow as a deposit or “backup". Their numbers diminish with age.
Ø The intermediate stage cells are like the pluripotent stem cells but are called
committed stem cells because their level of specialization increases.
Ø It is capable of both self-replication and differentiation to committed
precursors-cells that can produce only a specific cell line.
18
ØThe committed Red cell precursor undergoes several
divisions.
ØThe daughter cells becomes progressively smaller,
ØThe cytoplasm changes color from blue to pink as
hemoglobin concentration of about 34% is synthesized.
ØThe nucleus becomes small and dense and then
extrude/absorbed from the cell.
ErythropoiesisCFU-Erythroid
(CFU-E)cells
Early
Proerythroblast
(Pronormoblast)
Basophilic
Normoblast
Intermediate
Late
Polychromatophilic
Reticulocyte
Normoblast
Orthochromatophilic
Erythrocyte
Normoblast
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Erythropoiesis-CFU-Erythroblast
ØThe resulting non-nucleated cells is termed a reticulocyte since it still contains a
small amount of basophilic material, consisting of remnants of the Golgi
apparatus, mitochondria and a few other cytoplasmic organelles.
ØDuring this reticulocyte stage, the cells pass from the BM into the blood
capillaries by Diapedesis.
ØWithin a few(1-2) days of entering the circulation, the reticulocytes lose their
RNA(remaining basophilic material) and becomes Mature red cells(erythrocyte).
Early
Proerythroblast
(Pronormoblast)
Basophilic
Normoblast
Intermediate
Late
Polychromatophilic
Reticulocyte
Normoblast Orthochromatophilic
Normoblast
Erythrocyte
20
Genesis of normal RBCs and characteristics of RBCs in different types of Anemias.
Genesis of Blood Cells
Committed stem cells form
colonies of specific types of blood
cells.
CFU：colony-forming unit
•Erythrocytes = colony-forming unit–
erythrocyte = CFU-E.
•Granulocytes and monocytes come
from CFU-GM.
Growth and reproduction of the different stem cells are controlled by growth inducers.
•Differentiation of the cells, is controlled by differentiation inducers.
And this is controlled by factors outside the bone marrow. Via LOW oxygen, Infectious diseases cause the release of
mediators for growth and differentiation of specific types of WBCS to combat each type or stage of infection.
Importance of the Erythropoiesis
Ø Maintain the number of the red cells remarkable
constant.
Ø Anemia: due to
1)Decrease rate of erythropoiesis or increased rate of red
cells destruction, leads to
2)decreased number of red cells and weight of hemoglobin.
24
Regulation of Erythropoiesis
A. Erythropoietin,
Ø a glycoprotein released predominantly(90%) from the kidneys in response to tissue
hypoxia/hypoxemia.
Ø It also produced by Reticuloendothelial system of the liver and spleen.
Ø Erythropoietin Effect:
Ø 1) Stimulates the proliferation and differentiation of the committed red cell
precursor(Erythroblastosis)
Ø 2) Accelerates hemoglobin synthesis
Ø 3) Shortens the period of red cells development in the bone marrow.
Hypoxia-inducible factors-1&2(HIF-1,HIF-2) are essential mediators in cellular oxygen homeostasis,
facilitate both oxygen delivery and adaptation to O2
Levels by regulating the expression of gene products.
25
Regulation of Erythropoiesis
ØB. Other hormones stimulate erythropoiesis:
Ø1) Adrenal cortical steroids,
Ø2) Pituitary growth hormone,
Ø3) Parathyroid hormone
Ø4) Androgen
ØC. Estrogen – inhibit erythropoiesis.
• In a low tissue oxygen delivery situation, erythropoietin levels reach a maximum
in 24 hours.
• Almost no new RBCs appear in the circulating blood until about 3-5 days later.
• Erythropoietin stimulates the production of proerythroblasts from stem cells.
• Erythropoietin causes proerythroblasts to pass more rapidly through the
different stages than they usually do, speeding up the production of new RBCs.
26
Material for the RBC production.
• The protein and iron are used for Hemoglobin
synthesis.
• Both vitamin B12 and folic acid are necessary cofactors for DNA synthesis, which is essential for
maturation of the red cells.
27
Maturation of RBCs
• The erythropoietic cells of the bone marrow are among the most rapidly growing and
reproducing cells in the entire body, and their rate of production and maturation are greatly
affected by the nutritional status.
• Both vitamin B12 and folic acid are essential for the synthesis of DNA because each, in a
different way, is required for the formation of thymidine triphosphate, one of the essential
building blocks of DNA.
• Lack of either vitamin B12 or folic acid causes abnormal and diminished DNA and,
consequently, failure of nuclear maturation and cell division.
The erythroblastic cells, in addition to failing to increase rapidly, produce more prominent than
normal RBCs called macrocytes, which have a weak membrane and are irregular, large, and oval
instead of the usual biconcave disk.
• These cells can carry oxygen normally, but they have a short life span because of their fragility (one-half to onethird normal).
• These RBCs have a high:
MCV = MEGALOBLASTIC ANEMIA
• A common cause of RBC maturation failure is failure to absorb vitamin B12 from the gastrointestinal tract. This
situation occurs in the pernicious anaemia, in which there is an atrophic gastric mucosa that fails to
produce normal gastric secretions. (Autoimmune disease)
• The parietal cells of the gastric glands secrete a glycoprotein called intrinsic factor, which combines with vitamin
B12 in food and makes the B12 available for absorption by the gut. Intrinsic factor binds with vitamin B12 and
protects it from digestion by gastrointestinal secretions.
• Intrinsic factor binds to specific receptor sites on the brush border membranes of the mucosal cells in the ileum,
delivering B12 directly.
• Vitamin B12 is transported into the blood by pinocytosis, carrying intrinsic factor and the vitamin together through
the membrane.
• Lack of intrinsic factor decreases the availability of vitamin B12.
If vitamin B12 is ingested in its free (or nonprotein bound form), it will bind to a carrier protein known as R-binders
or transcobalamin I (Haptocorrin) that is secreted by both the salivary glands in the oropharynx and the gastric
mucosal cells within the stomach.
Vitamin-B12
• Vitamin B12 is stored in the liver and released as needed.
• The minimum amount of vitamin B12 required daily to maintain RBC
maturation is 1 to 3 micrograms.
• The average storage in the liver and other body tissues is about 1000 times
the daily needs.
• 3 to 4 years of defective B12 absorption are required to cause clinical
maturation failure anemia (Megaloblastic Anemia).
Folic acid
• Folic acid is a normal constituent of green vegetables, some fruits,
and meats (especially liver).
• It is easily destroyed during cooking.
• People with gastrointestinal absorption abnormalities, such as
patients with Tropical sprue, have difficulty absorbing folic acid and
vitamin B12.
• In many instances, the cause of megaloblastic anemia is the
deficiency of intestinal absorption of both folic acid and vitamin B12.
o -M m m o ie vu im icM cia
ALA
D ehydratase
P o rp h o b ilin o g e n
Deam inase
■ ■
aka
H ydroxym ethybilan e
Synthase
In h ib ited by Lead (Pb)
Acute Interm ittent Porphyria
•Autosomal dominant, late onset
• Episodic, variable expression
•Anxiety, confusion, paranoia
•Acute abdominal pain
• No ohotosensitivity
• Port-wine urine in some patients
Never give barbiturates
Cytochrome P450
Heme consumption
U roporphyrinogen III
[Hemej
Synthase
A No inhibition of ALA svnthase
Heme Synthesis (cont’d)
Porphyria Cutanea Tarda
• Most common porphyria
•Autosomal dominant, late onset
• Photosensitivitv
• Inflammation, blistering,
shearing of skin in areas
exposed to sunlight
• Hyperpigmentation
• Exacerbated by alcohol
Red-brown to deep-red urine
1 st p o rp h y rin o f pathw ay
E m g llp /j7 /j no il^ j
U ro p o rp h y rin o g e n
D e ca rb o xyla se
•Q Q jM Q iT J m
I
*
P ro to p o rp h y rin
Fe
i
IX
F e rro c h e la ta s e
Heme
....... n h ib ite d by Lead (Pb)
••**
........
A c q u ire d P orphyria:
r
P lum bism
.
If I Ferrochelatase or I Fe «=> Zn protoporphyrin (fluorescent)
Basic chemical steps in the formation of Hemoglobin.
• Succinyl-CoA binds with glycine to form a pyrrole molecule.
• Four pyrroles form protoporphyrin IX, which combines with iron to create the Heme molecule.
• Each heme molecule combines with a polypeptide chain, a globin, forming a subunit of
hemoglobin called a hemoglobin chain.
• Four of these chains bind together to form the hemoglobin molecule.
• There are variations in the subunit Hemoglobin chains, depending on the amino acid
composition.
• The different types of chains are designated alpha chains, beta chains, gamma chains, and
delta chains.
• The most common form of Hemoglobin in the adult human being, Hemoglobin A, is a
combination of two alpha chains and two beta chains.
Hemoglobin A2 (HbA2) is a normal variant of hemoglobin A that
consists of two alpha and two delta chains (α2δ2) and is found at low
levels in normal human blood.
Hemoglobin A2 may be increased in betathalassemia or heterozygous people for
the beta-thalassemia gene.
Iron in Hemoglobin
• Each Hemoglobin chain has a Heme prosthetic group containing an
atom of iron.
• There are four Hemoglobin chains, in each Hemoglobin molecule; so
there are four iron atoms in each Hemoglobin molecule.
• Each of these can bind loosely with one molecule of oxygen, making a
total of four molecules of oxygen (or eight oxygen atoms) that can be
transported by each hemoglobin molecule.
Iron Metabolism
Dietary
, .Fe
_ 3+
Vitam in
C
F e 2+
1 mg
4,300 Fe / protein
Storage protein
Muscosa
HFE
*
Carrier
|F e rritin | I Transferrin| Most
( h e J* )
Tissues
F e 2+
About 10% Fe is absorbed
Hemochromatosis
Hemosiderin deposits in:
Liver - cirrhosis
Pancreas - diabetes
Joints - arthritis
Skin - dermatitis
F e 2+
F e 3+
Bone
E ry th ro p o ie s is
B lood iron test:
TIBC = Total Iron-Binding Capacity
Transferrin should be 1/3 saturated
Ferritin
(F e 3+)
F e 2+
enzymes &
cytochromes
RES cells
Hb
RBC
= transferrin receptor
Iron absorption
• Iron absorption from the intestines is extremely slow.
• Of the iron present in the food, only small proportions can be absorbed.
• When the body is saturated with iron, and all apoferritin in the iron
storage areas is combined with iron, absorption from the intestinal tract
decreases.
• When iron stores are depleted, the absorption rate can accelerate five or
more times normal.
• Total body iron is regulated mainly by altering the rate of absorption.
Iron absorption and transport
• Iron in the small intestine combines with a beta globulin,
apo-transferrin, to form transferrin, which is transported in
the plasma.
• The iron is loosely bound in transferrin and can be released
to any tissue cell at any point in the body.
• Excess iron in the blood is deposited especially in the liver
and less in the reticuloendothelial cells of the bone marrow.
Storage Iron
• In the cell cytoplasm, iron combines with Apoferritin protein to form
ferritin(Fe3+).
• This iron stored as ferritin is called storage iron.
• Smaller quantities of iron in the storage pool are in a highly insoluble
form called hemosiderin.
• This happens when the total amount of iron in the body is more than
what the apoferritin storage pool can accommodate.
• Hemosiderin collects in cells in the form of large clusters that can be
observed microscopically as large particles. (Pathological –
Intracytoplasmic inclusions.).
IRON
METABOLISM
Iron metabolism
1) Iron is necessary for the formation of hemoglobin and other essential
elements in the body (e.g., myoglobin, cytochromes, cytochrome oxidase,
peroxidase, and catalase).
2)The total amount of iron in the body averages 4 to 5 grams:
65%in the form of hemoglobin.
4 % in the form of myoglobin.
1 % in the form of the various heme compounds in the mitochondria that
promote intracellular phosphorylative oxidation.
0.1 % is combined with transferrin in the blood plasma.
15-30 % is stored for later use, mainly in the reticuloendothelial system and liver
parenchymal cells, principally in the form of ferritin(Fe3+).
IRON METABOLISM
• When iron levels in the plasma fall, some of the iron in
the ferritin storage pool is removed and transported as
transferrin in the plasma to where it is needed.
• The transferrin molecule binds with receptors in the cell
membranes of erythroblasts and is ingested by
endocytosis, delivering iron directly to the mitochondria,
where heme is synthesized.
• Low transferrin in blood (Hypotransferrinemia) causes
severe hypochromic anemia).
Chloramphenicol
Glucocorticoids
Adrenocorticotropic hormone
Cirrhosis
Nephrotic syndrome
Kidney failure
Hemochromatosis
Hemolytic anemia
Sideroblastic anemia
Sickle cell disease
Congenital atransferrinemia
Hemoglobin
• The hemoglobin molecule must have the
ability to combine loosely and reversibly
with oxygen.
• The primary function of Hemoglobin in the
body is to combine with oxygen in the
lungs and then release this oxygen in the
peripheral tissue capillaries, where the
partial pressure of oxygen is lower than in
the lungs.
• Oxygen binds loosely with one of the socalled coordination bonds of the iron atom.
• This bond is extremely loose, so the
combination is easily reversible.
• The oxygen does not become ionic oxygen
but is carried as molecular oxygen.
Life-span of Red blood cells
• Mature RBCs do not have a nucleus, mitochondria, or endoplasmic reticulum;
they only have the enzymes to metabolize glucose and generate small ATP
amounts. (Glycolysis and Pentose cycle enzymes).
•Other RBC enzymes like G6PD:
(1) Maintain flexibility of the cell membrane.
(2) Maintain membrane transport of ions.
(3) Keep the iron of the cells hemoglobin in ferrous(Fe2+ rather than ferric(Fe3+)form.
(4) Prevent oxidation of the proteins in the RBCs.
•The metabolic systems of old RBCs become progressively less active, and the cells
become more and more fragile.
THE LIFE-SPAN OF RED BLOOD CELLS
1)The old RBCs rupture during passage through small spaces in the circulation.
2)Many RBCs self-destruct in the spleen, where they squeeze through the Red
pulp of the spleen, where the spaces between the structural trabeculae are only 3
mm wide, in contrast with the average 8mm diameter of the RBC.
3)Hemoglobin is released from them and is phagocytized by macrophages in the
reticuloendothelial system.
4)Macrophages release iron from hemoglobin and pass it into the blood, to be
carried by transferrin either to the bone marrow to produce new RBCs or to the
liver and other tissues for storage in the form of ferritin.
5) The porphyrin portion of the hemoglobin molecule is converted by the
macrophages, through a series of stages, into bilirubin, which is released into the
blood and removed by the liver into the bile.
Microcytic Anemia
• When hemoglobin synthesis is deficient, the % of hemoglobin in the
cell falls, and the volume of the RBC may also decrease because of
diminished hemoglobin to fill the cell.
Aplastic Anemia
• Bone marrow aplasia means a lack of functioning bone marrow. (Bone marrow insufficiency - Failure).
• Exposure to high-dose
radiation or chemotherapy for cancer treatment.
• Toxic chemicals, such as insecticides or benzene in gasoline.
• In autoimmune disorders like SLE.
• Pathogens.
• Idiopathic aplastic anemia.
Megaloblastic Anemia
1)Lack of vitamin B12, folic acid, and intrinsic factor can lead to slow development
of erythroblasts in the bone marrow.
2)The RBCs grow too large, with odd shapes, and are called megaloblasts.
3)Atrophy of the stomach mucosa, as in pernicious anemias, or loss of the entire
stomach after total surgical gastrectomy can lead to megaloblastic anemia.
4)Megaloblastic anemia often develops in intestinal sprue patients.
5)RBCs that are formed are mostly oversized, have bizarre shapes, and have fragile
membranes.
6)These cells rupture easily, leaving the patient with an inadequate number of
RBCs.
Hemolytic Anemia-Hereditary spherocytosis
1)Abnormalities of the RBCs, many of which are hereditary, make the cells fragile, so they
rupture easily as they go through the capillaries, especially through the spleen.
2) Even though the number of RBCs formed may be normal, or even much greater than normal
in some haemolytic diseases, the life span of the fragile RBC is so short that the cells are
destroyed faster than they can be formed, and serious anaemia results.
3)In Hereditary spherocytosis, the RBCs are very small and spherical rather than being biconcave
disks.
These cells cannot withstand compression forces because they do not have the normal loose,
bag like cell membrane structure of the biconcave disks.
Upon passing through the splenic pulp and some other tight vascular beds, they are easily
ruptured by even slight compression.
Hemolytic Anemia-Sickle cell Anemia
1) In sickle cell anemia, which is present in 0.3 - 1%of West African and American blacks.
2) In this amino acid valine is substituted for glutamic acid in each of the two beta chains and
form abnormal type of hemoglobin called hemoglobin S
3) When this type of haemoglobin is exposed to low oxygen,Hb precipitates into long crystals
inside the RBC that elongate the cell and give it the appearance of a sickle rather than a
biconcave disk.
• These crystals make it almost impossible for the cells to pass through many tiny capillaries. The
pointed ends of the crystals rupture the cell membranes, so the cells become highly fragile
leading to sickle cell anemia.
4) Patients with sickle cell anemia experience a vicious circle called a sickle cell disease “crisis,”
in which low oxygen tension in the tissues causes sickling, which leads to ruptured RBCs, which
causes a further decrease in oxygen tension and still more sickling and RBC destruction.
• Once the process starts, it progresses rapidly, in a severe decrease of RBCs within a few hours
and, in some cases, death.
III) Physical and Chemical Properties of the
Blood
III. Physical and Chemical Properties of the Blood
Ø1) Gravity
Ø Blood: 1.05-1.60
Ø Plasma: 1.025-1.030
Ø2) Suspension Stability of the Red Cells and
Erythrocyte sedimentation rate (ESR).
Ø3) Viscosity
Ø4) Plasma Osmotic Pressure
53
2) Suspension Stability of the Red Cells
ØThe Erythrocytes are very stable in suspension due to the repelling
force by the same (negative) charge of the red cells.
ØWhen the blood is anticoagulated and added in a narrow tube,
rouleaux of the red cells are formed and then its sediment gradually
takes place.
Ø The length of sedimentation of the red cells within one hour is termed
Erythrocyte sedimentation rate (ESR).
54
Erythrocyte sedimentation rate (ESR).
1) The normal range
• 0-3 mm per hour in men,
• 0 – 10 mm per hour in women.
2) Depends mainly on the relative concentration of the plasma protein (Albumins
and Globulins).
• Globulin and fibrinogen enhances the formation of the Rouleaux.
• Almost all the infections (especially the Tuberculosis and Rheumatism) that are
accompanied by a rise of globulin can accelerate ESR.
55
Viscosity(thickness/stickiness)
Ø The Frictional force between the elements in the blood.
Ø The Relative viscosity of the blood is 4-5, which is greater than that in
plasma (1.6 – 2.4) and water (1).
Ø The Higher the Red cell concentration and the amount of plasma protein,
the Greater the viscosity of the blood.
Ø Increase of the viscosity can enhance the peripheral blood
resistance(TPR), decreasing the blood supply to tissue.
56
Plasma Osmotic Pressure
• Osmosis: Net diffusion of the water across a semipermeable membrane to a
region in which there is a higher concentration of solute
57
Osmotic pressure.
ØThe osmosis of the water molecules can be opposed by applying a pressure in
direction opposite that of the osmosis.
ØThe precise amount of pressure required to prevent the osmosis is called the
osmotic pressure
ØThe total plasma osmotic pressure : 313 mOsm
ØIt consists of two parts.
1) The plasma crystal osmotic pressure
2) The plasma colloid osmotic pressure
58
1) Plasma crystal osmotic pressure
Ø 5305 mmHg (99.5%).
Ø formed from the crystal substances(Glucose,salt Na+) and in the plasma.
Ø plays an important role in maintaining water equilibrium between the
plasma and the intracellular fluid.
2) Plasma Colloid osmotic pressure
Ø 25 mmHg (0.5%).
Ø formed from the colloid substances and plasma proteins(Albumin) in
the plasma.
Ø Important to maintain the water equilibrium between the plasma
and the interstitial fluid.
59
Plasma osmolarity- Colloid osmotic pressure
• If the blood osmolarity is too high, the bloodstream absorbs too much
water, and blood volume and pressure will be elevated, placing strain
on the heart and vessels. (Hypervolemia and Hypertension).
• If osmolarity is low, excess water remains in the tissues, the patient
becomes edematous (swollen), and blood pressure may drop.
(Hypovolemia and Hypotension)
•Albumin is essential to maintaining optimal
osmolarity and optimal fluid balance.
Osmotic pressure.
ØIn clinical practice, it is common to substitute the term
tonicity for osmolarity when referring to solutions.
ØA solution is Isotonic (isosmotic) if a normal cell does not
change its volume when exposed to it.
ØThis solution has a same osmotic pressure as that of the plasma.
61
Example:1 A 0.9 percent solution of sodium chloride, called
physiological saline, or a 5 percent glucose solution is
Isotonic.
0.9% Na
99.1% H2O
solution
0.9% Na
99.1% H20
62
Ex:2 A solution that causes
shrinkage of the cell is called
hypertonic (hyperosmotic)
solution.
0.9% NaCl
99.1% H2O
Ex:3 A solution that causes
the cell to swell is termed
hypotonic (hypoosmotic)
solution.
solution
8% NaCl
92% H2O
0.9% Na
99.1% H2O
solution
0.5% Na
99.5% H2O
63
Thank you