Ch. 10 - Hemoglobin Metabolism (Incom. start at Hb synthesis...) Flashcards

1
Q

This is the first protein whose structure was described using x-ray crystallography.

A

Hemoglobin (Hb)

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

This molecule is a conjugated globular protein consisting of four heme groups and two heterogenous pairs of polypeptide chains.

A

Hemoglobin

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

The hemoglobin molecule has how many heme groups?

A

4

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

The hemoglobin molecule has how many heterogenous pairs of polypeptide chains?

A

2

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

This is the main cytoplasmic component of erythrocytes.

A

Hemoglobin (Hb)

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

This type of hemoglobin (Hb) is generated from RBCs through hemolysis; it has a short half-life, is rapidly salvaged and is catabolized or excreted renally.

A

Free (non-RBC) Hemoglobin (Hb)

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

What is the approximate concentration of hemoglobin within the RBCs?

A

34 g/dL

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

What is hemoglobin’s main function?

A

To transport oxygen from the lungs to the tissues.

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

Hemoglobin also modulates vascular dilation by transporting nitric oxide (NO) and transports _____ from the tissues to the lungs for exhalation.

A

Carbon dioxide

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

Heme consists of a ring of carbon, hydrogen, and nitrogen atoms called _____ with an atom of divalent ferrous iron (Fe2+) attached.

A

Protoporphyrin IX

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

Heme consists of a ring of _____, _____, and _____ atoms called protoporphyrin IX with an atom of divalent ferrous iron (Fe2+) attached.

A

Carbon
Hydrogen
Nitrogen

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

Heme consists of a ring of carbon, hydrogen, and nitrogen atoms called protoporphyrin IX with an atom of divalent _____ attached.

A

Ferrous iron (Fe2+)

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

Each heme molecule combines reversibly to how many oxygen molecules.

A

One

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

Each heme molecule combines (irreversibly/reversibly) to one oxygen molecule.

A

Reversibly

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

The four globin chains comprising each hemoglobin molecule consists of how many identical pairs of unlike polypeptide chains?

A

Two

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

The four globin chains comprising each hemoglobin molecule consists of two identical pairs of unlike polypeptide chains with how many amino acids each?

A

141 - 146

17
Q

Each globin chain is divided into how many helices and nonhelical segments?

A

Eight helices

Seven nonhelical segments

18
Q

This part of the globin chain is designated as A to H and contains subgroup numberings for the sequence of the amino acids in each helix and are relatively rigid and linear.

A

Helices

19
Q

This part of the globin chain connects the helices, as reflected by their designations.

A

Flexible nonhelical segments

20
Q

This hemoglobin structure refers to the amino acid sequence of the polypeptide chains.

A

Primary structure

21
Q

This hemoglobin structure refers to the chain arrangements in helices and nonhelices.

A

Secondary structure

22
Q

This hemoglobin structure refers to the arrangement of the helices into a pretzel-like configuration.

A

Tertiary structure

23
Q

This hemoglobin structure describes the complete hemoglobin molecule.

A

Tertiary structure, or tetrameric molecule

24
Q

Each globin chain contains a heme group that is suspended between the _____ and _____ helices of the polypeptide chain.

A

F and E

25
Q

The iron atom at the center of the protoporphyrin IX ring of heme is positioned between two _____ radicals, forming a proximal histidine bond within F8.

A

Histidine

26
Q

Globin chain amino acids in the cleft are (hydrophobic/hydrophilic) whereas amino acids on the outside are (hydrophobic/hydrophilic).

A

Hydrophobic

Hydrophilic

27
Q

(T/F) The hemoglobin molecule is water soluble.

A

T

28
Q

What is the shape of the complete hemoglobin molecule?

A

Spherical

29
Q

How many heme groups and polypeptide chains does the complete hemoglobin molecule have?

A

4; 4

30
Q

How many molecules of oxygen can the complete hemoglobin molecule carry?

A

4

31
Q

(T/F) The complete hemoglobin molecule is composed of 4 alpha globin chains and two non-alpha globin chains.

A

F (2-alpha globin chains)

32
Q

(T/F) Each heme group, attached to a globin chain, can carry multiple molecules of oxygen.

A

F (Only one molecule of oxygen per heme)

33
Q

Heme biosynthesis occurs in the _____ and _____ of bone marrow RBC preursors.

A

Mitochondria

Cytoplasm

34
Q

The production of globin chains takes place in _____ from the pronormoblast through the circulating polychromatic (polychromatophilic) erythrocytes.

A

RBC precursors

35
Q

(T/F) The production of globin chains can take place in mature RBCs.

A

F

36
Q

The combination of two a (alpha) and two B (beta) chains along with their four heme molecules forms what heemoglobin? This is the predominant hemoglobin in postnatal life.

A

Hemoglobin (Hb) A

37
Q

This type of hemoglobin contains two alpha and two delta chains; the delta chains are inefficiently expressed; only small amounts of this Hb are found in the RBCs.

A

Hb A2

38
Q

This type of hemoglobin contains two alpha and two gamma chains; in adults, this is distributed unevenly among RBCs.

A

Hb F; present in a few RBCs called F cells