21 Ass 11 Practicals Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

How would a researcher prepare the epidermis of leaves from crops to be viewed under a microscope 5

A

Gather a fresh sample of leaves from several crops

Tear the leaves and use forceps and gloves to cleanly peel away the epidermis

Place the epidermis on a clean slide on a drop of water

place a cover slide over this using a mounted needle and wipe away excess

stain if necessary

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Reagent and positive result in testing for starch

A

Iodine solution
Blue/black colour

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Reagent and positive result in testing for reducing sugars

A

Benedict’s reagent
green/yellow/orange/red colour

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Reagent and positive result in testing for non-reducing sugars

A

Boil with Benedict’s reagent after acid hydrolysis

darker colour

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What type of sugar is glucose?

A

reducing sugar

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What type of sugar is sucrose?

A

non-reducing sugar

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Define activation energy

A

Energy needed in a chemical reaction for a product to form

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What is an enzyme inhibitor?

A

Something that inhibits the rate of enzyme activity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What is a competitive inhibitor?

A

It has a similar shape to the substrate and temporarily fits into the enzymes active site, competing with the substrate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What can make a competitive inhibitor reversible?

A

Increasing the substrate concentration will reduce effect of inhibitor

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What is non-competitive inhibition? 2

A

It doesn’t bind to the active site, but another part of the enzyme

causing a change in the enzymes shape so it’s no longer complementary

Increasing substrate has no effect

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

(7) which graph shows the change in concentration of enzyme substrate complex?

A

A

not B bc not just concentration but CHANGE in concentration

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

How do you plot the initial rate of reaction? 3

A

draw a tangent to the curve at the start of the reaction

Find an easy- to read part of the scale to stop drawing

Make triangle as big as possible

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

How do you calculate the initial rate of reaction? 2

A

Calculate the gradient of line

Change y / change x

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What is activation energy

A

the energy level that must be overcome before a reaction can progress

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What is Vmax?

A

The point at on y-axis which the line of enzyme reaction is horizontal

17
Q

How do you calculate Km

A

1/2Vmax on y-axis & then find value on the X-axis

18
Q

Ass 2 3 b) fig 2.1 Describe & explain shape of curve 5

A

When substrate concentration is lower, rate of reaction is proportional to substrate concentration

This is because there are still some unoccupied active sites

At higher substrate concentrations, the increase in the rate of reaction is slower

& substrate concentration is no longer limiting factor, instead enzyme concentration is

because all active sites are occupied

19
Q

For a commercial application using an enzyme, the progress of the enzyme-catalysed reaction needs to be studied. Outline how the progress of an enzyme-catalysed reaction can be investigated experimentally 4

A

Keep temperature & pH constant

Take samples of the amount of product formed at regular intervals

Plot a graph of product formation against time

Draw a tangent to determine initial rate of reaction

20
Q

What is used to test for proteins

A

biuret solution

21
Q

What is used to test for lipids and positive result?

A

ethanol and milky emulsion/cloudy

22
Q

How do you convert mm to um?

A

x by 1000

23
Q

How does wavelength affect microscopy?

A

A shorter wavelength gives better resolution

24
Q

A specimen of plant tissue is observed twice with a microscope, first using a red light with wavelength of 650nm and then with green light using wavelength of 510nm what happens to the magnification & resolution when using green light compared to red light?

A

With a green light the magnification remains the same as the red light but the resolution increases

25
Q

q4 the diagram shows an eyepiece graticule and part of a stage micrometer scale as seen using x100 magnification. what is the correct method for calculating the value of one eyepiece graticule unit in micrometers (um)?

A

multiply 0.1 by 1000 then divide by 100

26
Q

A student observes a cell using a light microscope. The student then draws the cell. Which items will the student need to calculate the magnification of the drawing? 3

A

eyepiece graticule, ruler and a stage micrometer scale

27
Q

Describe the appearance of the centrosome

A

non-membrane bound cylindrical structures

28
Q

Describe the appearance of the ribosome

A

non-membrane bound, spherical structures

29
Q

How big are viruses?

A

20nm - 500nm

30
Q

How many nm in 1 mm?

A

1000 000

31
Q

Can a light microscope see a virus that’s 30nm in diameter?

A

No, because the virus is 30nm and a light microscope’s resolution is too low, and can only distinguish points 200nm or more apart

32
Q

What is the formula for calculating magnification?

A

I
AM

33
Q

How would one test for non-reducing sugars? 5

A
  1. add 5cm^3 of food fresh food sample to test tube
  2. boil food sample with hydrochloric acid
  3. Neutralise test solution by adding sodium hydroxide
  4. add 5cm^3 of Benedict’s reagent
  5. heat test tube in thermostatic water bath set to 80 degrees C for 3 min
34
Q

What does enzyme affinity mean? 2

A

A measure of how readily enzyme-substrate complexes form & lead to products

low affinity= substrate can leave active site without any reaction taking place

35
Q

What is meant by Km? 4

A

Michaelis-Menten Constant

can predict theoretical affinity of enzyme

value is substrate concentration at which enzyme works at 1/2 Vmax

lower Km=higher affinity bc Vmax reached at higher substrate concentrations & vice versa