Digestivstem

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  • Created by: Jenna k
  • Created on: 15-04-14 06:27
Descirbe the gross stuctrue of the digestive system.
Baccal cavity, Oesophagus, stomach, small intestines (ileum), large intestines (colon) and rectum.
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Name the two glands associated with digestion.
The savliary glands in the baccal cavity and the pancreaus below the stomach that secreats into the ileum.
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Define digestion.
Digestion is the process in which molecules are hydrolised by enzymes to produce smaller melecules that can be absorbed and assimilated.
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What's the difference between physical and chemical digestion?
Physical brakedown occures when learge molecules are brocken down by teeth, where as chemical digestion is when enzymes and chemicals react to fuel the hydrolosis reaction.
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Define Assimilation.
This is the process where molecules are hydrolised and absorbed into the blood stream by the epithilial cells in the small intestins. These then from larger molecules that are used in cells, but arent the same as the molecules they were dirived from.
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Name three enzymes.
Carbohydrase, Protease, Lipase and Hydroloase.
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Darw an alpha glucose monosaccharide.
.
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What bonds are formed by what reaction?
Glycosidic bonds are formed by a condecation reaction (water is removed) form C1-C4
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What is the disaccharide of Alpha glucose?
Moltose
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What is the enzyme for moltose
Moltase
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What is a polysacchiride of alpha glucose?
Startch
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Sucrose in the disacchirde of what?
Glucose and fructose
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Lactose is a disacchride of what?
Glucose and glactose.
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What is a monosacchired?
A single basic molecular unit form whichi carbohydrates are composed.
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What is a disacchride?
The condensation recation of two monosacchrides.
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What is a polysacchirde
A chain of Monosacchride units.
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What is the test for reducing sugars?
Benidicts test. Add Benidicts regant to the sample and heat for five minutes and if it turns brick red there is a reducion sugar present.
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What is the test for non-reducing sugars?
Add Benidicts solution to the sample and heat for 5 minutes. If turns blue then add hydorchloric acid to a new test tube and heat and then add soduim hydrocarbonate to nutrilise the HCL heat and retest with Benidicts solution if it turns brick red...
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Decribe the test for starch.
Add iodine to the sample. If it turns black then there is starch pressent.
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Describe starch digestion.
physical brakedown in baccal cavity.Amylase produce to hydrolise starch. Bolus in Oesophagus. HCL in stomach kill enyme. Ileum pancriotic amylase and moltase produced to further brake down. Assimilation in SI and excreated through the rectum.
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What is the enzyme for sucrose?
Sucrase
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What is the enzyme for lactose
Lactase
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State three method of testing for lactose intolerance.
Stoole test, Hydrogen test and the Lactose intolerance test.
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Describe the lactose intolerance test.
Patient fasts before and then takes a lactose solution. Blood sample are take afterwards to see if the blood sugars have increased. If the blood glucose does not rise then there is an intolerance.
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Describe the stoole test.
A stoole is collected and the acidity is measured. High acid- intolerance.
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Describe the hydrogen test.
Subject fasts and then drinks a lactose solution. If hydrogen levels increase the lactose is not being broken down but instead fermented and hydrogen is a biproduct.
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What is the differacne between primary and secondary lactose deficiency?
Primary developes as you age and is useually as a result of a faulty gene. Where as Secondary is as a results of an acident or disease causeing your body to not make enough lactase.
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Draw an amino acid
.
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How is a peptide bond formed?
Its a condesation reaction between Carboxyle and amino group.
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What is the primary structure of proteins?
A chain of amino acids.
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What is the secondary structure of proteins?
The hydrogen of the amino group becomes positively charged and the oxygen of the carboxyle group becomes negitively charged. They are attracted and hydrogen bonds form which cause a alpha helixical structure.
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What is the Tertiary structure of a protein?
This is an addition of the alpha helix where Disulfide, Iconic and hydrogne bonds form a large 3D structure.
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What is the quaternary structure of proteins.
This consists of 3-4 tertiary structures intwided together. With an addition of a prosthetic group.
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What is an example of a tertiray structure of protein?
Enzymes
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What is an example of a quanternary structure of protein?
Haemoglobin
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What is the test for proteins.
Biuret test. Consisting of adding Sodium hydroxide to the sample. Then adding silfate solution and mixing gentally. The result should dhow a purple coloration to indicate the presents of a peptide bond.
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What is the role of an enzyme?
It is a catalystes which lowers the activation energy throug formation of enyme substrate complexes.
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Describe the lock and key model of an enzyme.
The enzyme and the substrate are said to be complementrey so they fit together to form a enzyme-substrate complex.
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What is a limitation of the lock and key model?
Considered to be a ridged structure how everidance suggests it could be flexiable.
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Descirbe the incuded fit model of an enzyme.
This is where the enzyme is liek a glove to the substrate. It has a shape but hat shape can still mold to the substrate. So they are still complimentory and form an enzyme-substrate molecule.
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What are the factors effecting enzyme activity?
Tempriture, pH and concentration of substrates.
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How deos Tempriture affect enzyme activity.
Tempriture increases kenectic energy. So the rate of collision also increases meaning more enzyme-substrate complexes are being formed. However to much heat and the hydrogen bonds on the enzyme brakes and the enzyme denatures
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How does pH affect enzyme activity?
pH alters the changes on the active site and thus repels the substrate so enzyme substrate complelexs arent formed. Also it cause the bonds to brake within the enzyme causing it to denature.
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How does subsrate concentration affect enzyme activity?
If there is more substrate then there will be more collisions and more enzyme substrate complexes will be formed.
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What are inhibitors?
Inhibitors are molcules that bind to to enzyme and interfer with its process.
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What is a competitive inhibitor?
This inhibitor will bind to the active site of the enyme so the substrate cant.
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What is a non-competitive inhibitor?
This is an inhitor that binds to another part of the enzyme thats not the active site and slowly it denatures the enzyme so it cant bind with the substrates.
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Other cards in this set

Card 2

Front

Name the two glands associated with digestion.

Back

The savliary glands in the baccal cavity and the pancreaus below the stomach that secreats into the ileum.

Card 3

Front

Define digestion.

Back

Preview of the front of card 3

Card 4

Front

What's the difference between physical and chemical digestion?

Back

Preview of the front of card 4

Card 5

Front

Define Assimilation.

Back

Preview of the front of card 5
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