Mass transport in animals Flashcards
What is the structure of haemoglobin?
> Primary structure - sequence of amino acid in 4 groups -> alpha helix
Tertiary structure - formation of hydrogen bonds to form a specific shape
Quaternary structure - associated with heam group
How does haemoglobin release/carry oxygen?
Unloading - haemoglobin releases oxygen (disassociating)
Loading - haemoglobin attaches/binds to oxygen
Why do different species have different affinities?
Different primary structures, so H+ bonds form in different areas leading to a different tertiary structure leading to different affinities.
What happens further left on the oxygen dissociation curve?
> more loading occurs, due to a greater affinity for oxygen
What happens further right on the oxygen dissociation curve?
> Futher right: more unloading occurs, due to less affinity for oxygen
Why is it difficult for the 1st oxygen bind to hameglobin?
> Difficult for 1st haemoglobin to bind with oxygen; however, after binding this leads to changes in quaternary structure, leading to positive cooperativity.
What is the effect of carbon dioxide concentration?
> Lower carbon dioxide concentration, leads to more loading of oxygen and higher carbon dioxide concentration leads to more unloading of oxygen
Dissolved co2, lowers the ph - causes haemoglobin to change shape - more readily unlaods o2 - more oxygen available for respiration
What occurs during diastole?
> Diastole - relaxation of heart - blood flows into atria, pressure increases in the atria, which cause atrioventricles valves to open and blood to flow to ventricles. Semi-lunar valves close
What occurs during atristole systole?
Atrial systole - atria contracts allowing the rest of the blood to flow into ventricles, recoil of ventricle walls - ventricle walls relaxed.
What occurs during ventricular systole?
After a short delay, the walls contract, and pressure increases in the ventricles, which causes atrio-ventricular valves to close (preventing backflow) and semi-lunar valves to open, causing blood to be pushed in PA, or aorta.
Cardaic output = ________ x __________
a. heart rate
b. stroke volume
Structure and function of arteries:
> carries blood away from the heart, a thicker wall - withstand high BP,
muscular layer, thick elastic layer - control blood flow
Structure and function of veins:
carries blood towards the heart, valves to prevent the backflow of blood, a thinner wall - lower pressure, elastic layer and a thinner muscular layer
Structure and function of capillaries:
Narrow diameter, narrow lumen, slow blood through narrow lumen allowing for more time for diffusion, highly branched = larger SA:vol
Structure and function of arterioles:
Control flow of blood from arteries to capillaries. Thicker muscular layer than arteries to withstand high Bp, thinner muscular layer than arteries
Pocket valves:
in veins - ensure blood flows back towards heart
Structure of heart:
Vena cava (deoxygenated blood from body) -> Right atrium -> AV valve -> Right Ventricle -> pulmonary artery (carries deoxugenated blood to lungs) -> pulmonary vein (returns oxygenated blood from lungs) -> aorta (oxygenated blood - body)
What are some adaptations of atrium?
thin walled and elastic - stretches as it collects blood
What are some adaptations of the ventricle?
thicker wall - strongly pump and contract
What are the coronary arteries?
supplies o2 to heart
Explain how water from tissue fluid is returned to the circulatory system.
Plasma proteins remain in the blood as they are too large to diffuse which creates a water potential gradient and lowers the water potential in the blood. Water diffuses by osmosis and is later returned to the circulatory system via the lymphatic system
Explain how an arteriole can reduce the blood flow into capillaries.
Muscle in arterioles contracts which narrows the lumen
Describe the structure of haemoglobin.
Globular, water soluble, conatins 4 polypeptides chains
What are 3 factors affecting oxygen-haemoglobin binding?
- partial pressure of oxygen
- partial pressure of carbon dioxide
- saturation of haemoglobin with o2