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Biochem HLS > Lec 2 > Flashcards

Lec 2 Flashcards

1
Q

What is hemeprotien ?

A

Polypeptide chain with heme group

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2
Q

What is the role of heme group in cytochrome & catalase & hemoglobin?

A

Cytochrome: electron carrier
Catalase : catalyze the breakdown of hydrogen peroxide
Hemoglobin:bind to oxygen

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3
Q

Heme structure ?

A

Protoporphyrin IX and FE in the center

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4
Q

Myoglobin consist of how many polypeptide chain ?

A

1

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6
Q

One polypeptide of hemoglobin or myoglobin consist of how many alpha helical structure?

A

8 , A B C D E F G H

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7
Q

Which bond stabilizing alpha helix of myoglobin polypeptide?

A

Hydrogen bond & ionic bond

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8
Q

Interior of myoglobin consist of ?

A

Non polar amino acid which make hydrophobic bond to packed and stabilize the structure

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9
Q

Surface of myoglobin consist of ?

A

Polar amino acid which stabilize the structure by hydrogen bond

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10
Q

Proximal histidine occurs at ?

A

F alpha helix and bind directly to FE

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11
Q

Distal histidine occurs at ?

A

E alpha helix and bind to oxygen which bind to Fe (indirect)

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12
Q

What is the main role of hemoglobin?

A

Transport oxygen

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13
Q

How many oxygen cal hemoglobin transport?

A

Four

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14
Q

What is the interaction between alpha & beta in the dimmer ?

A

Hydrophobic

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15
Q

What is the interaction between two dimmers?

A

Hydrogen & ionic bond

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16
Q

T form of hemoglobin is deoxy or oxy hemoglobin?

A

Deoxyhemoglobin

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17
Q

How many oxygen does T form of hemoglobin carried ?

A

Zeroooo

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18
Q

In any form there are many hydrogen bond?

A

T form

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19
Q

Which form of hemoglobin have higher affinity to oxygen and which one have lower?

A

R form have higher and T form have lower

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20
Q

What is the change that occurs after bind oxygen to hemoglobin ?

A

Interdimer interaction or ionic & hydrogen bond will broken which lead to more free movement of polypeptide chane

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21
Q

Hitch one have high affinity to oxygen ? Hemoglobin or myoglobin?

A

Myoglobin

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22
Q

What is the shape of dissociation curve of myoglobin?

A

Hyperbolic shape

23
Q

What is the shape of dissociation curve of hemoglobin?

A

Sigmoid also shape

24
Q

Why hemoglobin make sigmoidal dissociation curve ?

A

Due to allosteric effect

25
Q

What is the allosteric effect

A

Binding of one oxygen to hemoglobin increase hemoglobin affinity to other atoms of oxygen

26
Q

Which molecules of oxygen is more difficult to bind to hemoglobin ? And which one have the easiest one ?

A

First one have the difficult and last one have the easiest due to allosteric effect

27
Q

Increased metabolites lead to shift curve to ? And why

A

Shift to right because increase co2 , acidity, temperature and 2,3-BPG which lead to decrease affinity to oxygen

28
Q

2,3-BPG bind to detox or oxy hemoglobin?

A

Deoxyhemoglobin

29
Q

2,3-BPG decreased or increased affinity of oxygen ?

A

Decreased and shift curve to right

30
Q

Where 2,3BPG bind on hemoglobin?

A

On beta chain , on positive amino acid such as histidine & lysine because it have negative charge

31
Q

In pregnancy, the affinity of oxygen increased or decreased?

A

Decreased because increased 2,3-BPG about 30%

32
Q

Which hemoglobin have higher affinity to oxygen?Hb A or HB F? And y

A

HB F because it doesn’t affected by 2,3-BPG

33
Q

HB F shift curve to ?

A

Leeeeeeft

34
Q

Met HB & co HB shift curve to ?

A

Leeeeft

35
Q

HB A2 consist of ? And when it appears

A

2 alpha & 2 delta , and appears after 12 weeks(3month) of birth

36
Q

HB A2 increase in thalassemia or sickle cell anemia?

A

It increased in thalassemia and still normal on sickle cell anemia

37
Q

Which type of HB use to measure blood glucose?

A

HB A1c

38
Q

What is hemoglobinopathies?

A

group of disorders passed down through families (inherited) in which there is abnormal production or structure of the hemoglobin molecule

39
Q

What is fatal hemoglobin?

A

This occurs when HB F fall to convert to HB A

Fall gamma to convert to beta

40
Q

What is sickle cell anemia?

A

Point mutation in gene for beta globin

41
Q

Any type of anemia produced by sickle cell anemia?

A

Hemolytic anemia (destruction of red blood cell)

42
Q

What is the abnormal amino acid in sickle cell anima?

A

Valine which get place glutamate

43
Q

Whcich one has more negativity? HB A / HB S / HB C ? And why ?

A

HB A because glutamate have negative charge where as valine is neutral (HB S) and lysin have positive charge (HB C)

44
Q

What is HB C ?

A

Hemoglobin which glutamate in position 6 replaced by lysine

45
Q

Any type of anemia does HB C have ?

A

Hemolytic anemia

46
Q

Beta thalassemia minor ?

A

Defective of one gene that produced beta globin (heterozygous)

47
Q

Cooley anemia?

A

Beta thalassemia major , which have defer in two beta gene (which produced beta globin)

48
Q

Beta thalassemia?

A

Mutation in chromosome number 11 , in beta gene which lead to insufficient beta globin

49
Q

Alpha thalassemia ?

A

Defect on chromosome 16 , alpha gene , which lead to insufficient alpha chain

50
Q

What is HB H ?

A

Hemoglobin consist of 4 beta chain , this result from alpha thalassemia when 3 gene of alpha get mutation and this cause moderate hemolytic anemia

51
Q

What is HB Bart?

A

Hemoglobin consist of 4 chain of gamma , this produced due to alpha thalassemia in which 4 alpha gene get mutation

52
Q

What is primaquine drugs ?

A

This drug use to kill malaria , this drugs mustn’t be used in patients with G6PD deficiency

53
Q

Which two of alpha helix bound with FE ?

A

F bind directly by histidine amino acid , E indirectly by bind to oxygen and oxygen bind to Fe

Biochem HLS (3 decks)

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