University of Guyana

Faculty of Natural Sciences

Department of Biology

BIO3220 – Animal Physiology

Laboratory Exercise # 5
Haemin Crystals.

Name of Student
Naiomi Persaud

Date of Submission:
April 17, 2020
Title: Haemin Crystals

Aim: To investigate the different structures and their functions found within the Haemin crystals.

Materials:

 Blood samples from a cow.

 Blood samples from a chicken.
 Crystal of common salt (NaCl).
 Acetic acid.

Apparatus:

 Glass slide.
 Glass rod.
 Cover slip.
 A spirited lamp.
 Microscope.

Method:

1. A small amount of dry blood was placed on a glass slide and crushed to a fine powder
with the help of a fused end of a glass rod.
2. One crystal of common salt (NaCl) was added to the glass slide, which was also crushed
to powder.
3. The two were thoroughly mixed and two drops of acetic acid was added.
4. The mixture was covered with a cover slip and the slide was heated over a flame of a
spirited lamp.
5. The reaction was considered complete with the beginning of the boiled mixture and slide
was quickly removed from the flame.
6. The preparation was allowed to cool before it was examined under the microscope,
initially under low magnification and then high.
Results
Discussion

The purpose of this laboratory experiment was the investigate the different structures of haemin
crystals found within a blood sample taken from a farm and sanctuary mammal (cow) and bird
(chicken). Biological organisms are reliant on blood to carry out various biological processes
such as homeostasis. These blood cells are also known as erythrocytes. They can be defined as
specialized cells delivering oxygen to cells by circulation (Randall et al., 1980). These cells are
generated from stem cells in the bone marrow. The erythrocytes are relatively small and
biconcave shaped without a nucleus or mitochondria in mammals. In comparison to birds and
reptiles, the nucleus is still present in these erythrocytes (Randall et al., 1980). These cells are
made up of haemoglobin which is known to bind with oxygen and transport it around the body.
Haemoglobin is also responsible for the red colouring of blood and has iron-containing protein
(Randall et al., 1980). Haemoglobin can be considered an important protein molecule found in
erythrocytes which is transported around the bodies of vertebrates, movement of oxygen from
the lungs to tissues that require it most. All kingdoms of organisms are found to possess
haemoglobin within their blood (Sanyal et al., 2013).

Biologists have studied the molecules of haemoglobin of vertebrates in great detail and found
that the ancestral gene for haemoglobin was proved to originated from bacterial cells and has
evolved to eukaryotes (Sanyal et al., 2013). The structural and functional properties of
haemoglobin structure have shown to be dependent on adaptations to environment factors and
physiological demand of the species. Haemoglobin was noted to perform other functions aside
from the transport of oxygen around the bodies of biological organisms (Sanyal et al., 2013). It
was also shown to have varying oxygen carrying capacity in the different kingdoms of
organisms. The haemoglobin of reptiles displays reduced oxygen transport ability and the
cardiovascular system show low fluid resistance which can be caused by widely spaced
capillaries (Randall et al., 1980). In the group of fishes, the haemoglobin concentration is
dependent of the environment the fish is present in, this depends on the fresh or saltwater
environment. Birds and mammals share similar haemoglobin structure but the difference occurs
in the high oxygen affinity that birds require to adjust when present in high altitudes (Sanyal et
al., 2013). This laboratory experiment compares the differences of haemoglobin between within
a blood sample taken from a farm and sanctuary mammal and bird.
The purpose of adding the crystal of common salt (NaCl) and acetic acid was to bind to the
haemoglobin so the shape can be easily identified during observation. Under the microscope, the
blood of the mammal was observed to have haemin crystals which were noted to have are brown
colour rectangular with sharp edges projecting outwards which is breadth (Sengupta, 2012). In
mammals, haemoglobin can be described as a tetrameric molecule which means that it is
comprised of four subunits and consists of two alpha- and two beta-polypeptide chains. These
polypeptide chains contain one haem group (Sanyal et al., 2013). The shape and structure of the
alpha and beta chains is dependent on the amino acid sequence of the species. The shape of the
crystals was projected by the folding of two alpha- and two beta-polypeptide chains. Each
molecule of haemoglobin is then responsible for oxygen transport or any other necessary
biological functions (Sanyal et al., 2013). In comparison the blood sample of the bird, under the
microscope the blood yields hemin crystals which resemble in shape a sheaf of wheat bound in
the middle, flanged and twisted at the ends and red blood cells are seen to be nucleated
(Sengupta, 2012). In birds, haemoglobin can be described as a as a minor component found
within the erythrocytes. The haemoglobin was also found to be made of up an alpha-d globin
structure which allows for the high oxygen affinity that allows this organism to adapt to high
altitudes (Sanyal et al., 2013). Although the shape and structures of haemoglobin can be seen to
be similar under the microscope, there are minute differences which are dependent on the alpha-
two beta-polypeptide chains and alpha-d globin structure.

Conclusion

In conclusion the functional differences between the haemin crystals observed in the blood
samples from the mammal and bird is mostly due to the alpha D globin which has a similar
structure to the tetrameric molecule of haemoglobin in mammals (Sanyal et al., 2013). The alpha
D globin structure has allowed birds to be able to adapt to hypoxic conditions. The hemoglobin
molecule properties were also seen to be dependent and influenced by environmental conditions
across the kingdoms of organisms (Sanyal et al., 2013).
References

Randall, D., Burggren, W., & French, K. (1980). ANIMAL PHYSIOLOGY MECHANISMS AND
ADAPTATIONS. 8(4), 417–426. https://doi.org/10.1111/1540-6229.00227

Sanyal, M., Patil, P., Jaiswal, E., & Deshmukh, A. (2013). Structural and functional diversity of
haemoglobin molecule properties amongst different classes and species of animals. Acta
Biologica Indica, 2(2), 381–387.

Sengupta, P. Das. (2012). Comparative studies of Haemin crystal of Mammals- Structural and
Statistical Analysis. 2(12), 1–6.