Topic 3B- More Exchange and Transport Systems Flashcards
Why are large molecules of food broken down into smaller molecules during digestion?
Because the large biological molecules are too big to cross cell membranes, meaning they cant be absorbed from the gut into the blood
What is amylase?
Amylase is a digestive enzyme that catalyses the conversion of starch into the smaller sugar maltose (a disaccharide).
How does amylase convert starch into maltose?
Hydrolysis of the glycosidic bonds in starch
Where is amylase produced?
Salivary glands, pancreas (releases amylase into small intestine)
What are carbohydrates broken down by?
amylase and membrane-bound disaccharidases
What are membrane-bound disaccharidases?
enzymes that are attached to the cell membranes of epithelial cells lining the ileum. They help to break down disaccharides into monosaccharides. (involves hydrolysis of glycosidic bonds)
How are lipids broken down?
Lipase (with the help of bile salts)
What are lipids broken down into?
monoglycerides and fatty acids
What bonds are broken in lipids as they are broken down?
ester bonds
Where are lipids made, and where do they work?
made- pancreas
work- small intestine
Where are bile salts produced?
the liver
What is the purpose of bile salts?
They emulsify lipids (cause lipids to form small droplets). This means there is a larger SA:V ratio, for a faster rate of reaction
What happens once the lipid has been broken down?
The monoglycerides and fatty acids stick with the bile salts to form tiny structures called micelles.
What are proteins broken down by?
Endopeptidases and exopeptidases
Where do endopeptidases hydrolyse the protein’s peptide bonds?
within the protein
Give two examples of endopeptidases, and describe where they occur
trypsin and chymotrypsin
synthesised in the pancreas and secreted in the small intestine
What is pepsin an example of and describe it.
endopeptidase
Its released into the stomach by cells in the stomach lining. Pepsin only works in acidic conditions- these are provided by hydrochloric acid in the stomach.
Where do exopeptidases hydrolyse the protein’s peptide bonds?
Exopeptidases act to hydrolyse peptide bonds at the ends of protein molecules. They remove single amino acids from proteins
What are dipeptidases?
Exopeptidases that work specifically on dipeptides. They act to separate the two amino acids that make up a dipeptide by hydrolysing the peptide bond between them.
Where are dipeptidases located?
In the cell-surface membrane of epithelial cells in the small intestine
Where are the products of digestion absorbed into the blood?
Across the ileum epithelium in the bloodstream
How are monosaccharides absorbed into the blood?
Glucose and galactose- absorbed by active transport with sodium ions via a co-transporter protein
Fructose- absorbed via facilitated diffusion through a different transporter protein
Why can whole micelles not be taken up across the epithelial cell membrane?
because they constantly break up and ‘reform’ they can ‘release’ monoglycerides and fatty acids, allowing them to be absorbed.
How do monoglycerides and fatty acids travel across the epithelial cell membrane?
They are lipid soluble so can diffuse straight across
How are amino acids absorbed?
co-transport (sodium ions, active transport)
Explain how amino acids are absorbed during co-transport
sodium ions actively transported out of ileum epithelium into blood
creates a sodium ion concentration gradient
sodium ions can then diffuse from lumen of the ileum into the epithelium cells through sodium-dependent transporter proteins, carrying amino acids with them
What is haemoglobin?
a large protein with a quaternary structure
each polypeptide chain has a haem group, which contains an iron ion, gives it red colour
Why is haemoglobin useful for carrying oxygen?
It has a high affinity for oxygen- each molecule can carry four oxygen molecules
What reaction occurs in the lungs and body between oxygen and haemoglobin?
oxygen joins to haemoglobin to form oxyhaemoglobin, reversible reaction
How can you measure oxygen concentration?
the partial pressure of oxygen
What does a greater partial pressure mean?
the greater the concentration of dissolved oxygen in cells, the higher the partial pressure
What is does the partial pressure of CO2 measure?
the concentration of CO2 in a cell
Describe the movement of oxygen using haemoglobin
oxygen loads onto haemoglobin to form oxyhaemoglobin where there’s a high pO2
oxyhaemoglobin unloads its oxygen where there’s a lower pO2
What level of pO2 do alveoli have?
high
What does a dissociation curve show?
how saturated the haemoglobin is with oxygen at any given partial pressure
On a dissociation curve, what does 100% saturation show?
that each haemoglobin molecule is carrying the maximum of 4 molecules of oxygen
What does 0% saturation mean on a dissociation curve?
none of the haemoglobin molecules are carrying any oxygen
What happens when pO2 is high?
haemoglobin has a high affinity to oxygen, so it has a high saturation of oxygen
What happens when pO2 is low?
haemoglobin has a low affinity for oxygen, which means it releases oxygen rather than combines with it
Why is the dissociation curve S-shaped?
The graph is S-shaped because when haemoglobin (Hb) combines with the first O2 molecule, its shape alters in a way that makes it easier for other molecules to join too. But as the Hb starts to become saturated, it gets harder for more oxygen molecules to join, so curve has a steep bit in the middle where it is really easy for molecules to join, and shallow bits at each end where it’s harder. When the curve is steep, a small change in pO2 causes a big change in the amount of oxygen carried by the Hb
What is haemoglobins affinity affected by?
higher partial pressures of CO2 means haemoglobin gives up its oxygen more readily
Why is the Bohr effect useful during physical activity?
more oxygen can get to cells in lower pO2