Mass Transport in animals Flashcards
Describe the structure and functions of haemoglobins
Haemoglobins are protein molecules whose tertiary structure allows for efficient loading of oxygen under one set of conditions and unloading under another:
primary - order of amino acids joined by peptide bonds;
secondary - alpha helix/beta pleated sheet, hydrogen bonds;
tertiary - specific 3D structure. hydrogen bonds, ionic bonds, disulphide bonds;
quaternary - 4 polypeptide chains;
quaternary - prosthetic haem group;
Explain the differences between haemoglobins in different organisms and the reasons for these differences
Different organisms have haemoglobin with different amino acid sequences, therefore, different tertiary and quaternary structures which affects affinity for oxygen
association/loading of oxygen
the process by which haemoglobin binds with oxygen
dissociation/unloading of oxygen
the process by which haemoglobin releases oxygen
Describe and explain the shape of the oxyhaemoglobin dissociation curve
-In low partial pressures haemoglobin has a low affinity for oxygen (dissociates oxygen more easily), the curve is shallow
-Curve becomes steeper as the affinity for oxygen increases
-Curve levels off at nearly 100% saturation at high partial pressures of oxygen - haemoglobin has a high affinity for oxygen (dissociates less easily)
Explain how binding of oxygen affects the shape of haemoglobin
-Hard for first oxygen to bind as haem groups are in the middle of the haemoglobin molecule
-First oxygen causes a conformational change in the haemoglobin (change in shape) making it easier for the second and third molecules to bind
-Harder to reach final binding site so fourth oxygen binds less easily
Describe and explain the Bohr effect
-Haemoglobin has a reduced affinity for oxygen in the presence of carbon dioxide.
-This means it loads oxygen less readily and unloads more easily.
-Dissolved carbon dioxide is acidic and this causes haemoglobin to change shape.
-At gas exchange surfaces there is little carbon dioxide, affinity for oxygen in high, oxygen loads readily.
-At respiring tissues carbon dioxide concentration is high, affinity for oxygen is low, oxygen is readily unloaded.
Explain how, with reference to haemoglobin, animals are adapted to their environment
An animal that lives in an environment with low partial pressure of oxygen will have haemoglobin with a high affinity for oxygen, the curve is to the left - this allows fully saturated haemoglobin at low partial pressures of oxygen
Explain why large animals have a transport system
Large animals have a small SA:volume and therefore have specialed exchange surfaces. Transport system is required to take substances from the exchange surfaces to all of the cells in the body
Describe the features of a transport system in large organisms
A medium to carry materials (eg blood).
A form of mass transport to move the medium in bulk.
A closed system of vessels to tranport the medium to all areas of the body.
A mechanism to move the medium in vessels
Describe the pattern of blood circulation in a mammal
Closed, double circulatory system. Deoxygenated blood is pumped to the lungs from the heart, oxygenated blood flows back to the heart and then is pumped around the body.
What affects whether organisms have a specialised transport medium and whether it is circulated by a pump?
Activity of the organism
SA : volume
Lower SA : volume and higher activity – greater need for specialised system with a pump
cardiac muscle
makes up the wall of the heart and is a thick muscular layer
properties of cardiac muscle
-myogenic
-never fatigues as long as it has a supply of oxygen
coronary arteries
supply the cardiac muscle with oxygenated blood