More Exchange And Transport Systems Flashcards
Why can’t we absorb large biological molecules (starch,proteins) during digestion from gut into blood?
- Too big to cross cell membranes so broken down into smaller molecules (glucose,amino acids) by hydrolysis reactions
- So can move across cell membranes and be easily absorbed
What are Carbohydrates, Fats and Proteins broken down into by hydrolysis?
- Carbohydrates> disaccharides and then monosaccharides
- Fats>fatty acids and monoglycerides
- Proteins>amino acids
What do digestive enzymes do?
- Glands produce enzymes that hydrolyse large molecules in food into smaller ones for absorption
- Variety of different digestive enzymes are produced by specialised cells in digestive systems of mammals
- Enzymes work with specific substrates so different enzymes catalyse breakdown of different food molecules
Amylase (digestive enzyme)
- Catalyses breakdown of starch by catalysing hydrolysis that breaks down glycosidic bonds to produce maltose (disaccharide)
- Produced by salivary glands which release amylase into the mouth
- Produced by pancreas which releases amylase into small intestine
What are Membrane-bound disaccharides and what do they do?
- Enzymes that are attached to the cell membranes of epithelial cells lining the ileum (final part of small intestine)
- They help break down disaccharides into monosaccharides by hydrolysis of glycosidic bonds
What are Carbohydrases, Lipases and Proteases?
- Carbohydrases>carbohydrates to monosaccharides
- Lipases>lipids to glycerol and fatty acids
- Proteases>proteins to amino acids
What is a monoglyceride?
A glycerol molecule with one fatty acid attached
What disaccharidases are involved in digestion?
How are monosaccharides transported?
Across the epithelial cell membranes in the ileum via specific transporter proteins
Lipase enzymes
- Catalyse breakdown of lipids into monoglycerides and fatty acids which involves hydrolysis of ester bonds
- Mainly made in pancreas and secreted into small intestine
Bile Salts and Micelles
- Produced by liver and emulsify lipids (cause them to form small droplets)
- Increases surface area of lipid that’s available for lipases to work on
- Once lipid has been broken down by lipase, the monoglycerides and fatty acids stick with bile salts to form tiny structures called micelles
- Micelles help products of lipid digestion be absorbed (help move monoglycerides and fatty acids towards epithelium)
- Micelles constantly break up and reform so they can release monoglycerides and fatty acids, allowing them to be absorbed as they are lipid soluble and can diffuse directly across epithelial cell membrane (whole micelles not taken up across epithelium)
How are proteins digested?
- By a combination of different peptidases (proteases)
- Catalyse hydrolysis of peptide bonds between amino acids
Endopeptidases
Act to hydrolyse peptide bonds within a protein
Exopeptidases
Act to hydrolyse peptide bonds and the ends of protein molecules. They remove single amino acids from proteins.
Dipeptidases
- Exopeptidases that work specifically on dipeptides
- Hydrolyse peptide bond between 2 amino acids
Where are Dipeptidases located?
Located on cell-surface membrane of epithelial cells in the small intestine (if located here, also called membrane-bound dipeptidases)
How are monosaccharides absorbed across ileum epithelium into bloodstream?
- Glucose is absorbed by active transport with sodium ions via co-transporter protein
- Galactose is absorbed in the same way using the same co-transporter protein
- Fructose is absorbed via facilitated diffusion through a different transporter protein
How are amino acids absorbed across ileum epithelium into bloodstream?
- Sodium ions are actively transported out of the epithelial cells into ileum itself
- They then diffuse back into cells through sodium-dependent transporter proteins in the epithelial cell membranes, carrying amino acids with them
What does Mass transport do?
Ensure efficient movement of substances over large distances throughout organisms to get them to their exchange surfaces
Role and structure of Haemoglobin
- In humans, found in red blood cells and carries oxygen
- Chemically similar types found in different organism but same function carried out
- Large protein with quaternary structure- made up of 4 polypeptide chains (2a and 2b)- coiled into helix
- Each chain has a haem group which contains and iron iron and gives haemoglobin its red colour
- Each haemoglobin can carry 4 oxygen molecules
Formation of Oxyhaemoglobin/Unloading and Loading
- In the lungs, oxygen joins to haemoglobin in red blood cells to form oxyhaemoglobin (reversible reaction)
- Near body cells, oxygen leaves oxyhaemoglobin and it turns back to haemoglobin
- Loading-oxygen joins haemoglobin
- Unloading-oxygen leaves oxyhaemoglobin He + 4O2 ~ HbO8
What is affinity for oxygen and how does it vary?
- Tendency a molecule has to bind with oxygen
- Haemoglobin’s affinity for oxygen varies depending on the conditions it’s in such as pO2
What is partial pressure of oxygen (pO2)?
Measure of oxygen concentration, greater concentration means higher partial pressure
What happens when pO2 increases/is high or low?
- Haemoglobin’s affinity for oxygen increases
- High pO2>oxygen loads on haemoglobin to form oxyhaemoglobin
- Low pO2>oxyhaemoglobin unloads oxygen
What happens at alveoli in lungs and respiring tissue?
- Oxygen enters blood capillaries at the alveoli in the lungs
- Alveoli has a high pO2 so oxygen loads onto haemoglobin to form oxyhaemoglobin
- When cells respire they use up oxygen which lowers pO2
- Red blood cells deliver oxyhaemoglobin to respiring tissues, where it unloads oxygen
- Haemoglobin then returns to lungs to pick up more oxygen
Villi properties
- Increase surface area for diffusion
- Thin walls and microvilli
- Contain muscle so are able to move
What does an oxygen dissociation curve show?
How saturated the Haemoglobin is with oxygen at any given partial pressure
What affects how saturated haemoglobin is?
Affinity of haemoglobin for oxygen
Explain the oxygen dissociation curve
- When pO2 is high (lungs), haemoglobin has a high affinity for oxygen, so high saturation of oxygen
- When pO2 is low (respiring tissues), haemoglobin has a low affinity for oxygen, so low saturation of oxygen
Why is oxygen dissociation curve S-shaped?
Saturation of haemoglobin can also affect affinity
What is the partial pressure of CO2?
Measure of concentration of CO2 in a cell
How does pCO2 affect oxygen unloading?
Haemoglobin gives up its oxygen more readily at a higher pCO2 so they can get more oxygen to cells during activity
What is the Bohr effect?
- When cells respire they produce carbon dioxide which raises the pCO2
- This increases rate of oxygen unloading-so dissociation curve shifts right (but it stays same shape)
- Saturation of blood with oxygen is lower for a given pO2, meaning that more oxygen is being released
Describe Bohr effect on curve
- Further to left, greater affinity of haemoglobin for oxygen (so it loads oxygen readily but unloads it less easily)
- Further to the right, lower affinity of haemoglobin for oxygen (so it loads oxygen less readily but unloads it more easily)
Why does haemoglobin have different oxygen transporting capacities?
- Depends on where the live, how active they are and size
- Having particular type of haemoglobin is an adaptation that helps organism to survive in particular environment
Curve in low oxygen environments
- Haemoglobin with higher affinity for oxygen than human haemoglobin because their isn’t much oxygen available (haemoglobin needs to be good at loading oxygen)
- Dissociation curve is left to ours
Curve with high activity levels
- Have lower affinity for oxygen than human haemoglobin because of high oxygen demand
- Need haemoglobin to easily unload oxygen, so it’s available for use
- Dissociation curve is right to ours
Curve relating to size
- Small mammals have higher surface area to volume ratio, so they lose heat quickly
- Need a high metabolic rate, so they have high oxygen demand (high respiration rate)
- Mammals smaller than human have haemoglobin with lower affinity for oxygen than humans
- Need to easily unload oxygen to meet high demand
- Dissociation curve is right to ours
How pH changes transport of oxygen?
- pH raises due to low concentration of CO2
- High pH change makes haemoglobin load oxygen readily
- Shape also increases affinity for oxygen so not being released when transported to tissues
- In tissues, CO2 is produced by respiring cells (CO2 is acidic and lowers pH)
- Low pH changes shape of haemoglobin so it has a lower affinity for oxygen
Why do multicellular organisms like mammals need a specialised mass transport system?
Have a low surface area to volume ratio
What is the Circulatory System made of?
- Heart and blood vessels
- Heart pumps blood through blood vessels (arteries,arterioles,veins and capillaries)
Pulmonary artery
Carries deoxygenated blood from heart to lungs
Pulmonary vein
Carries oxygenated blood from lungs to heart
Aorta
Carries oxygenated blood from heart to body