more exchange and transport systems B Flashcards
what is digestion
hydrolysis of large insoluble molecules to smaller soluble molecules (often polymers to monomers)
what are the substrates and products of carbohydrate digestive enzymes
-amylase -> starch into smaller polysaccharides
-maltase -> maltose into 2x glucose
-sucrase-> sucrose into glucose and fructose
-lactase-> lactose into glucose and galactose
which enzymes are involved in carbohydrate digestion and where are they found
-amylase in mouth
-maltase, sucrase, lactase in membrane of small intestine
state the digestion of starch process
-amylase hydrolyses starch to maltose
-amylase produced by salivary glands,released into mouth
-amylase produced by pancreas, released into small intestine
-membrane bound maltase-> hydrolyse maltose to glucose
-hydrolysis of glycosidic bond
state the digestion of lipid process
- Bile salts produced by the liver
- Bile salts emulsify lipid to smaller lipid droplets
- Increasing surface area of lipids speeds up action of lipases
- Lipase made in the pancreas, released to small intestine
- Lipase hydrolyses lipids → monoglycerides + fatty acids
- Breaking ester bond
- Monoglycerides, fatty acids and bile salts stick together to form micelles
Describe the processes involved in the absorption and transport of digested lipid molecules from the ileum into lymph vessels
- Micelles contain bile salts and fatty acids/monoglycerides
- Make fatty acids/monoglycerides more soluble in water
- Fatty acids/monoglycerides absorbed by diffusion
- Triglycerides are formed in cells
- Vesicles move to cell membrane
Explain the advantages of lipid droplet and micelle formation
- Droplets increase surface areas for lipase / enzyme action
- So faster hydrolysis / digestion of lipids
- Micelles carry fatty acids and glycerol to cell
which enzymes are involved in protein digestion and what is their role
-endopeptidase=Hydrolyse peptide bonds between amino acids in the middle of the polypeptide
-exopeptidase=Hydrolyse peptide bonds at the ends of protein molecules
-dipeptidase= Hydrolyse peptide bond between a dipeptide and produces single amino acids
explain co transport of glucose and sodium ions
- Na+ actively transported out of epithelial cells by Na+/K+ pump into blood
- Establishes concentration gradient, as there is a higher conc of Na+ ions in the lumen of the intestine than inside the epithelial cells
- Na+ and glucose move by facilitated diffusion down conc gradient via co-transporter proteins into epithelial cell
- Glucose diffuses out of the cell into the blood plasma by facilitated diffusion using another type of carrier protein
why do fatty acids and monoglycerides not require co transport
molecules are non polar, meaning they can diffuse easily across the membrane of epithelial cells
what is the role of haemoglobin
to carry oxygen around the body
where is haemoglobin found in humans
red blood cells
why are red blood cells good for haemoglobin storage
- No nucleus – contain more haemoglobin
- Biconcave shape – increase surface area for rapid diffusion/absorption of oxygen
what is the structure of haemoglobin
- Quaternary structured protein – made of 4 polypeptide chains
- Each polypeptide chain contains a Haem group containing an iron ion (Fe2+) which combines with oxygen
what is meant by affinity for oxygen
ability of Hb to bind and release oxygen
describe the unloading of oxygen in regions with low pO2- respiring tissues
- Hb has a low affinity for O2
- So O2 readily unloads / dissociates with Hb
- So % saturation is low
describe the loading pf oxygen with high pO2- gas exchange surfaces
- Hb has a high affinity for O2
- So O2 readily loads / associates with Hb
- So % saturation is high
Describe how haemoglobin is involved in absorbing oxygen in the lungs and transporting it to respiring tissues
- diffusion of oxygen into red blood cells
- in lungs high pO2 so hb has high affinity for O2 so O2 binds readily to haem group forming oxyhaemoglobin -fully saturated
- in tissues low pO2 and hb has low affinity for O2 so unloads readily from haem group - low saturation
- in respiring tissues there’s a increase in pCO2 so dissociation curve shifts to right ( bohr effect) so affinity for O2 is even lower
The blood leaving a muscle has a lower pH than the blood entering it. During vigorous exercise, the fall in pH is even greater. Explain what causes this greater fall in pH
- in exercise there is a faster respiration rate
- more CO2 produced
- CO2 is acidic/ forms carbonic acid
- lactic acid production
- release of H+ ions = fall in pH (becomes more acidic)
How does the cooperative nature of oxygen binding result in an S-shaped (sigmoid) oxyhaemoglobin dissociation curve
- Binding of first oxygen causes Hb to change shape / tertiary / quaternary structure
- Which uncovers Haem group binding sites
- Making further binding of oxygens easier
what are the effects of CO2 conc on dissociation of oxyhaemoglobin : Bohr effect
- Increasing blood CO2 eg. due to increased rate of respiration
- Lowers blood pH (more acidic)
- Reducing Hb’s affinity for oxygen as shape / tertiary / quaternary structure changes slightly
- So more / faster unloading of oxygen to respiring cells at a given pO
what is the advantage of oxygen dissociation curve for oxyhaemoglobin shifting to the right
more oxygen for muscles/tissues for aerobic respiration → produce more ATP eg. for muscle contraction
Explain why the gradient of the oxygen dissociation curve is shallow initially
shape of haemoglobin makes it difficult for first oxygen to bind so at low oxygen partial pressures little oxygen binds
Explain why the gradient of the oxygen dissociation curve steepens after the first molecule of oxygen has bound
binding of the first oxygen changes the tertiary structure of haemoglobin making it easier for subsequent oxygen molecules to bind.
Explain why the gradient of the oxygen dissociation curve flattens off after the third oxygen has bound.
with the majority of binding sites occupied it is less likely that a single oxygen molecule will find an empty site to bind to
explain the adaptations of haemoglobin in organisms in low O2 environments
- Curve shifted left → haemoglobin has a higher affinity for oxygen
- More oxygen associates with haemoglobin more readily (in the lungs) at the lower pO2 BUT dissociates less readily
- Advantageous to organisms such as those living in high altitudes, underground, or foetuses
explain the adaptations of Haemoglobin in organisms in high O2 environments
- Curve shifted right → haemoglobin has a lower affinity for oxygen
- Oxygen dissociates from haemoglobin more readily to respiring cells at a higher pO2 BUT associates less readily
- Advantageous to organisms such as those with a high rate of respiration (metabolic rate) e.g. small / active organisms
Explain why large animals have a transport system
-Large animals have a small SA:volume and therefore have specialised 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 transport the medium to all areas of the body.
-A mechanism to move the medium in vessels”
what is pulmonary circulation
Deoxygenated blood in right side of heart pumped to lungs → oxygenated blood returns to left side of hear
what is systemic circulation
Oxygenated blood in left side of heart pumped to tissues / organs of body →
deoxygenated blood returns to right side
what is a closed double circulatory system
blood enclosed in vessels and passes twice through the heart for each circuit of the body
describe the general pattern of blood circulation in a mammal
- Deoxygenated blood in right side of heart pumped to lungs; oxygenated returns to left side
- Oxygenated blood in left side of heart pumped to rest of body; deoxygenated returns to right