Protein lab test

1.Which of the following chemicals did we use during fluorescenrt staining?

ona adasTRITC DAPI formaldehyde

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2. the sample buffer contains
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Glycerol mercaptoethanol bromphenol blue

3. I want to pipette 15 ug of proteins into the well. My sample has a concetration of 5 ug/ul.
I have mixed my sample with sample buffer in a ratio of 1:1. How many ul of the mixture do I
need to pipette into the well?

6 ul

4. we can visualize separated proteins in the gel using:

Commasie brilliant blue

5. to denature proteins in protein lysate, we do not use:

TEMED formaldehyde

6. what happened during centrifugation of the tissue samples in the lysis buffer?

Two phases appeared in the tubes: the supernatant containing the dissolved proteins was
the top phase, the pellet containing non-lyzed tissue was the bottom phase.

7. as a permeabilizing reagent, we can use

Triton X-100

8. mercaptoethanol

Is a denaturing reagent affects the proteins in the same way as dithiothreitol 9.

which unit can we use to describe the size of protein

KDa Da

10. sort the phases of the experiment from the beginning to the end

Triton X-100 – PBS for the first time -TRITC – PBS for second time- DAPI – flurosent microsc

11. to initiate the polymerization of acrylamide, we did not use:

SDS TRIS

12. to disintegrate the cells, we commonly use:

A lysis buffer
13. imagine that you have…. Myosin 210 kDa HPRT 25 kDa actin 43kDa proinsulin 11kDa

Proinsulin HPRT actin myosin

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14. Bovine serum albumine

Can be used to block the binding sites on he membrane in the method western

blot Can be used for making the solutions with a known protein concentration Can

be used to block binding sites on the membrane in the method SDS PAGE 15.

during the SDS-PAGE the proteins migrate:

To the positive electrode

16. the centrifugation of the samples creates:

Two phases: the upper one is called supernatant and contains protein

The lower one is called pellet contains non dissolved parts of the cell

17. the comassie brilliant blue

Can be used for the determination of the protein concentration in the

sample Stains the proteins in a non specific way

18. our sample contains a protein that consists of three subunits, which differ in size: A B
and C….. and run the SDS PAGE
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After SDS-PAGE, the subunits will form three separate bands.

19. before the SDS-PAGE, the proteins get a charge thankes to:

SDS

20. As a denaturing factor, we can use:

Dithiothreitol

Boiling

21. we cut the tissue into very small pieces to:

Enlarge the surface of the tissue exposed to the lysis buffer

22. I need to pipette 20 ug of proteins to the well. My sample has a concertation of 10 ug/ul.
I have mixed my sample with sample buffer in a ratio of 1:1. How many ul of the mixture do I
need to pipette into the well?

4 ul

23. the sample contain four proteins: dynamin 120 kDa myosin 210 kDa actin 42 kDa
HSP27 27 kDa …… SDS-PAGE How will the proteins become sorted ?
Myosin dynamin like protein actin HSP27

24. to prepare a stacking gel, we used a solution of:

Acrylamide
25. which fluorophores have we used for the fluorescent staining?

TRITC DAPI

26. the colour of Bradford reagent is:

Brown-green, after adding proteins, it turns blue.

27. we performed Bradford method:

At room temperature

28. we denature proteins before SDS-PAGE

At the temperature that does not preserve their enzymatic activity 29. which cell

structures did we stain during fluorescence staining? by which color?

Microfilaments (red) and DNA (blue)

30. we isolate proteins from cells and tissues at the temperature

That inhibits proteases

31.A unit of protein concentration is:

Mg/ml

32.We express the absorbance in

Absorbance has no unit

33. sort the following steps of protein lysate preparation into the correct order:

1.Cut the frozen tissues into small pieces

2. transport the small pieces of tissues into the micro tubes containg lysis buffer 3.

incubate the tissue pieces

4. centrifuge the microtubes

5. pipette the supernatants

6. dilute the samples

7. determine the protein concentrations using….

34. to specifically detect the protein of interest, we can use:

Bovine serum albumin comassie brilliant blue

35. to initiate acrylamide polymerization, we used:

APS SDS TEMED