HEMOGLOBIN

Nimra Faraz
DPT
 DEFINITION
Hemoglobin is the IRON containing PROTEIN compound within red blood cells
that carries OXYGEN throughout the body .
STRUTURE
Hemoglobin is a large protein molecule folded around four iron atoms
and it has a quaternary structure . A quaternary structure is where two or
more polypeptide chains join could be ionic , covalent or hydrogen bonds
.
In hemoglobin there are four polypeptide chains , each one of these
polypeptide chains contains a heme group which is able to bind to one
oxygen molecules .therefore four oxygen molecules can transported by
each hemoglobin molecule .
In every red blood cell there are approximately 270 million hemoglobin
molecules and so each red blood cell can carry about 1080 million
oxygen molecules .
Structure of hemoglobin
HEME MOLECULE
 TYPES OF HEMOGLOBIN
 There are Seven types of hemoglobin molecules througout a human’s life ,
four when you are an embryo , One once you develop into a fetus and then
as an adult you have two .
EMRYONIC HEMOGLOIN
 The form of hemoglobin most common and highest in proportion in
an embryo is Hemoglobin Gower I. The four polypeptide chains that
compose this type of hemoglobin are two Zeta and two Epsilon
chains.
The other three hemoglobin are present at much lower level :
 Hemoglobin Gower II composed of two Alpha and two Epsilon chains .
 Hemoglobin Portland I comprised of two Zeta and two Gamma
polypeptides.
 Hemoglobin portaland II made of Zeta and two Beta polypeptide
chains .
FETAL HEMOGLOBIN
Once the embryo develops into fetus and the four types of
embryonic hemoglobin molecules disappear they are
replaced by hemoglobin F.
This type of hemoglobin is used due to it having a great
affinity for oxygen than adult hemoglobin .therefore the
growing fetus is able to take its mother’s oxygen which is
in her bloodstream .
ADULT HEMOGLOBIN
Hemoglobin F remain in child’s blood until it is around six
months old and then almost all of it replaced with adult
hemoglobin
 • Hemoglobin A: it has two Alpha chains and two Beta
chains .
Hemoglobin A2 : it has two Alpha polypeptides and
two Delta polypeptides.
Hemoglobin A is most prevalent as it makes up about
97% of adult hemoglobin .
HEMOGLOBIN SYNTHESIS
Hemoglobin synthesis requires the coordinated production of
Heme and Globin . Heme is prosthetic group that mediates
reversible binding of Oxygen by Hemoglobin . Globin is the
protein that surrounds and protects the heme molecules .
ROLE OF HEMOGLOBIN
The role of hemoglobin is rather similar to a delivery truck
driver . The is because hemoglobin loads oxygen , transports
oxygen and then finally unloads it .
the process by which hemoglobin loads oxygen is called
associating , and this occurs in region of high oxygen
concentration – the lungs . Here the oxygen and hemoglobin
combine forming oxyhemoglobin .
• The process in which hemoglobin unloads oxygen is
called disassociating and occurs in regions of low
oxygen concentration – in tissues.
Here oxyhemoglobin splits back into oxygen and
hemoglobin
Oxygen + Hemoglobin
Oxyhemoglobin
THANK YOU !