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Haemoglobin and Gas Transport

Total questions: 29

Worksheet time: 18mins

Name
Class
Date
1.

the regular arrangement of amino acids in a linear sequence

a)

primary structure

b)

secondary structure

c)

tertiary structure

d)

quaternary structure

2.

function of myoglobin

(a)  

3.

how many polypeptide chain does myoglobin have?

a)

single

b)

two

4.

the number & types of polypeptide units and their spatial arrangement

a)

primary structure

b)

secondary structure

c)

tertiary structure

d)

quaternary structure

5.

Oxidized Hb is called as

(a)  

6.

what is Q?

a)

proximal histidine

b)

distal histidine

7.

how many percentage of protein in a healthy man of 65 kg?

a)

20%

b)

17%

c)

30%

d)

19%

8.

What haemoglobin contain 2a and 2b chain?

a)

HbF

b)

HbA

c)

HbA2

d)

HbA1

9.

what is P?

a)

distal histidine

b)

proximal histidine

10.

which globular protein has higher affinity towards oxygen?

a)

myoglobin

b)

haemoglobin

c)

deoxygenated haemoglobin

11.

in cyanide posoining,met-Hb can strongly bind to this and can sequester the circulating cyanide and prevent it from inhibiting electron transpost.

a)

H+

b)

H2SO4

c)

CN-

d)

CO

12.

what explain the steep of the haemoglobin curve in O2-Hb dissociation curve?

a)

affinity of O2

b)

cooperative binding

c)

binding of CO2

13.

which form of haemoglobin is when there is binding with oxygen?

a)

T form

b)

R form

14.

What happen to 2,3-BPG in COPD patients,high altitude,and in chronic anemia?

a)

remain unchaged

b)

increase

c)

decrease

15.

the binding of an O2 molecule at one haem group increase the 02 affinity of the remaining haem groups in the same Hb molecule,this effect is reffered as

(a)  

16.

which allosteric effectors below is homotropic?

a)

pH

b)

pCO2

c)

temperature

d)

availability of 2,3-BPG

e)

pO2

17.

Carbon dioxide is transported as

a)

carbaminohaemoglobin

b)

bicarbonate ions

c)

carbamate

d)

dissolved

18.

Which of the following decrease the affinity of Hb by binding to deoxy-Hb that stabilized the T form.

a)

lactate

b)

2,3-bisphosphoglycerate

c)

H+

19.

What happen when CO bind to Hb iron?

a)

Hb shift to R form

b)

changes sigmoid curve to hyperbola

c)

shift the O2 saturation curve to the left

d)

affected Hb has high affinity toward O2

20.

What can happen in Bohr effect?

a)

increase in pCO2

b)

pH is reduced

c)

decrease in O2 affinity of Hb

d)

the curve is shift to the right

21.

Why HbF has higher affinity to O2 compared to HbA?

a)

bcs the foetus blood is not mix with the mother

b)

to get the nutrients

c)

better access to oxygen from the mother's bloodstream

22.

what increase in B thalassemia?

a)

HbF

b)

HbA

c)

HbA2

d)

myoglobin

23.

Which is increased in diabetes mellitus?

a)

HbF

b)

HbA

c)

HbA1c

d)

HbA2

24.

which thalassemia only have one defective B-globin gene

a)

a-thalassemia

b)

B-thalassemia trait

c)

B-thalassemia minor

d)

thalassemia

25.

In Hbs,glutamine is replaced with

(a)  

26.

In haemoglobin C disease,a single amino acid,lysine is substituted for

(a)  

27.

What is the lifetime of HbS

a)

50 days

b)

50 years

c)

20 days

d)

120 days

28.

what happen in haemoglobin H disease?

a)

1/4 a-globin gene defect

b)

2/4 a-globin gene defect

c)

3/4 a-globin gene defect

d)

all four a-globin gene defect

29.

what happen in B-globin chain in hemoglobin SC disease

a)

all defect

b)

some B-globin gene have sickle cell mutation

c)

some B-globin gene carry mutation found in HbC disease

d)

some B-globin gene have sickle cell mutation and other have HbC disease mutation