Structure of Erythrocytes

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“STRUCTURE OF ERYTHROCYTES”

Presenter

DR.FARHAN ABID RANA


PGD FMU 2024-2026
ERYTHROCYTES

 Erythrocytes (red blood cells or RBCs) are anucleate,


biconcave cells, filled with hemoglobin, that transport
oxygen and carbon dioxide between the lungs and tissues.
They are produced in the red bone marrow by a process
called erythropoiesis.
 These mature RBCs are released into the bloodstream,
where they survive between 100 to 120 days.
FEATURES
 Erythrocytes have a consistent diameter of 7-8 µm.
 Erythrocytes have a biconcave shape, which resembles a
donut.
 Erythrocytes do not have a nucleus (anuclear) or any other
intracellular organelles.

 Only two major structures left are the cytoplasm which is


enclosed by a surrounding cell membrane
a) CYTOPLASM- contains the hemoglobin
b) CELL MEMBRANE- lipid bilayer containing peripheral and
integral proteins
Hemoglobin
 Hemoglobin is a complex iron-containing protein found in erythrocytes (red blood
cells) of most vertebrates that plays a vital role in carrying oxygen and carbon
dioxide within the blood..

 Beside RBC, hemoglobin is also present in alveolar cells, macrophages, some neurons
of the midbrain, mesangial cells of kidneys, hepatocytes, vaginal epithelial and
cervical cells, etc.

 Hemoglobin is synthesized together with the red blood cells (RBCs) during
erythropoiesis in the bone marrow. The iron part (heme part) is synthesized in the
cytoplasm and mitochondria of developing RBC and the protein part (globin protein)
is synthesized by the ribosome of the growing RBC

 Oxygen + Hemoglobin = Oxyhemoglobin 98%

 Carbondioxide + hemoglobin = Carbaminohemoglobin 2-3%


 ALLOSTERY
 Hgb is a globular metalloprotein with a quaternary structure. One
hemoglobin molecule is composed of four subunits; each containing
one polypeptide chain (chain of globin protein) attached with a
prosthetic heme group

 The polypeptide chains in adults are of two types, the alpha


chain and the beta chain containing 141 and 146 amino acids
respectively. Adult hemoglobin has two alpha subunits (α1 and
α2) and two beta subunits (β1 and β2)

 Each subunit has a heme attached to the globin protein

 In fetal hemoglobin, the beta subunits are replaced by gamma


subunits (γ1 and γ2).

 The heme group contains an iron (ferrous ion, Fe+2) held in the
center of a porphyrin ring binding with the nitrogen atoms of
the ring. The Fe+2 ion is bound to the pocket of the globin
subunit with a histidine residue. Each Fe +2 ion can bind with one
oxygen (O2) molecule or one carbon dioxide (CO 2) molecule

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