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CCL2P1

Total questions: 42

Worksheet time: 21mins

Name
Class
Date
1.

arrangement or sequence of amino acid in the polypeptide

a)

primary protein structure

b)

secondary protein structure

c)

tertiary protein structure

d)

quarternary protein structure

e)

Functional protein

2.

- local repeated pattern/ local folding og the polypeptide chain into helices or sheets

- due to hydrogen interaction among amino acid

a)

primary protein structure

b)

secondary protein structure

c)

tertiary protein structure

d)

quarternary protein structure

e)

Functional protein

3.

- three dimensional IRREGULAR and UNPREDICTABLE protein

- based on the side chain interaction

- May be functional

a)

primary protein structure

b)

secondary protein structure

c)

tertiary protein structure

d)

quarternary protein structure

e)

Functional protein

4.

- more than 1 chain

- protein consisting of more than 1 amino acid chain

a)

primary protein structure

b)

secondary protein structure

c)

tertiary protein structure

d)

quarternary protein structure

e)

Functional protein

5.

- should have at least 2,3, or 4 to be functional

a)

primary protein structure

b)

secondary protein structure

c)

tertiary protein structure

d)

quarternary protein structure

e)

Functional protein

6.

- Catalyzes redox reduction

- enzyme end with dehydrogenase

a)

Oxidoreductases

b)

Transferases

c)

Hydrolases

d)

Lyases

e)

Isomerases

7.

- carry or transfer amino group

- any enzyme that end with transferase

a)

Oxidoreductases

b)

Transferases

c)

Hydrolases

d)

Lyases

e)

Isomerases

8.

- enzyme that destroy bond in the presence of water

- the hydrogen and oxygen from water will saturate the end product

- No double bond

- end with ase

a)

Oxidoreductases

b)

Transferases

c)

Hydrolases

d)

Lyases

e)

Isomerases

9.

- do not require water to destroy bonds

- have double bonds

- end with ase

a)

Ligases

b)

Transferases

c)

Hydrolases

d)

Lyases

e)

Isomerases

10.

- enzymes that convert positional and geometric isomers

- still produce the same substances

a)

Ligases

b)

Transferases

c)

Hydrolases

d)

Lyases

e)

Isomerases

11.

- enzymes that connect or bind to substrate

- requires energy (ATP) during the linking

- have synthase or synthases at the end of the name

a)

Ligases

b)

Transferases

c)

Hydrolases

d)

Lyases

e)

Isomerases

12.

* First order of kinetics

a)

Substrate/ Enzyme Concentration

b)

pH and temperature

c)

cofactors

d)

inhibitors

13.

* the reaction or rate of reaction is HIGH if the enzyme is greater than the substrate

a)

First order kinetics

b)

Zero order kinetics

c)

Secondary order kinetics

14.

* If enzyme is fewer/ lesser than the amount of substrate

* become constant or dependent only in the amount of the enzyme ratio

a)

First order kinetics

b)

Zero order kinetics

c)

Secondary order kinetics

15.

* Denaturation

a)

Substrate/ Enzyme Concentration

b)

pH and temperature

c)

cofactors

d)

inhibitors

16.

* non substrate substances that binds to the enzyme (on the allosteric side)

* non protein entities MUST bind to enzymes for the reaction to occur

a)

Substrate/ Enzyme Concentration

b)

pH and temperature

c)

cofactors

d)

inhibitors

17.

* will always interfere or slow down an enzymatic reaction

a)

Substrate/ Enzyme Concentration

b)

pH and temperature

c)

cofactors

d)

inhibitors

18.

* competes with the original substrate or active site

* once it reach the enzyme first, the enzyme wont be available for binding

a)

Competitive Inhibitor

b)

Noncompetitive Inhibitor

c)

Uncompetitive

d)

Mixed Inhibitor

19.

* binds other sites

* all areas except the active site

* can be metabolize - REVERSE

a)

Competitive Inhibitor

b)

Noncompetitive Inhibitor

c)

Uncompetitive

d)

Mixed Inhibitor

20.

* KABIT

* wait for the formation of the substrate in the active site of enzyme and will bind the complex

* formation of product is unlikely to happen

a)

Competitive Inhibitor

b)

Noncompetitive Inhibitor

c)

Uncompetitive

d)

Mixed Inhibitor

21.

* either bind the substrate or enzyme but will not bind the complex

* will alter enzymatic reaction

*unlikely to work properly

a)

Competitive Inhibitor

b)

Noncompetitive Inhibitor

c)

Uncompetitive

d)

Mixed Inhibitor

22.

measure the end point

a)

fixed time

b)

kinetic/ continous monitoring

23.

1IU is equal to

a)

18 Nanokatals

b)

17 Nanokatals

c)

15 Nanokatals

d)

20 Nanokatals

24.

Distribution: Liver, Heart, skeletal muscle, kidney, pancreas, RBC

RF: 5 - 35 IU/L

a)

Aspartate aminotransferase (AST)

b)

Alanine aminotransferase (ALT)

25.

Distribution: Liver (higher concentration), widely distributed but small activity in other organs

RF: 7 -45 IU/L

a)

Aspartate aminotransferase (AST)

b)

Alanine aminotransferase (ALT)

26.

Avoid hemolysis

- affect result about 7000 types

refrigerate serum: 3-4days

a)

Aspartate aminotransferase (AST)

b)

Alanine aminotransferase (ALT)

27.

unaffected by hemolysis

Refrigerate serum: 3 - 4 days

a)

Aspartate aminotransferase (AST)

b)

Alanine aminotransferase (ALT)

28.

unaffected by hemolysis

Refrigerate serum: 3 - 4 days

a)

Aspartate aminotransferase (AST)

b)

Alanine aminotransferase (ALT)

29.

Substrate: P-nitrophenyl phosphate

Measurable end product: P-nitropgenil (405nm)

a)

Bessy, Lowry and Brocks/ Bowers - McComb

b)

Shinowara

c)

King Armstrong

d)

Huggins and Talalay

e)

Moss

30.

unaffected by hemolysis

Refrigerate serum: 3 - 4 days

a)

Aspartate aminotransferase (AST)

b)

Alanine aminotransferase (ALT)

31.

Substrate: B-Glycerophosphate

Measurable end product: Glycerol

a)

Bessy, Lowry and Brocks/ Bowers - McComb

b)

Shinowara

c)

King Armstrong

d)

Huggins and Talalay

e)

Moss

32.

Substrate: Phenylphosphate

Measurable end product: Phenol

a)

Bessy, Lowry and Brocks/ Bowers - McComb

b)

Shinowara

c)

King Armstrong

d)

Huggins and Talalay

e)

Moss

33.

Substrate: Phenolphthalein Diphosphate

Measurable end product: Red Phenolphthalein

a)

Klen Babson and Reed

b)

Shinowara

c)

King Armstrong

d)

Huggins and Talalay

e)

Moss

34.

Substrate: Alpha napthylphosphate

Measurable end product: Alpha naphthol

a)

Klen Babson and Reed

b)

Shinowara

c)

King Armstrong

d)

Huggins and Talalay

e)

Moss

35.

Substrate: Buffered phenolphthalein phosphate

Measurable end product: Phenolphthalein

a)

Klen Babson and Reed

b)

Shinowara

c)

King Armstrong

d)

Huggins and Talalay

e)

Moss

36.

Lung Cancer

- Phenylalanine placental, intestinal

a)

Regan

b)

Nagao

c)

Kasahara

37.

adenocarcinoma

- Phenylalanine, L-lysine

a)

Regan

b)

Nagao

c)

Kasahara

38.

Hepatoma

- no chemical inhibitor

a)

Regan

b)

Nagao

c)

Kasahara

39.

- All pregnancy

- Preeclampsia and eclampsia

- 16 to 20 weeks = 1-2x elevation

- 3rd trimester = 2 -3x elevation

a)

Placenta

b)

Liver

c)

Bone

d)

Intestine

40.

- biliary obstruction

- hepatocellular injury (slight)

- metastatic carcinoma of the liver

a)

Placenta

b)

Liver

c)

Bone

d)

Intestine

41.

- paget's disease

- rickets

- healing fractures

- hypophosphatasia

a)

Placenta

b)

Liver

c)

Bone

d)

Intestine

42.

- colon cancer

- type O and B secretors

- chronic hemodialysis

a)

Placenta

b)

Liver

c)

Bone

d)

Intestine