HEMOGLOBIN PART 1

Question 1

is the most common yet complex organic molecule in vertebrates, and also the most studied protein.

Answer 1

Hemoglobin

Question 2

is carried by RBCs in order for it to be protected.

Answer 2

Hemoglobin

Question 3

is carried inside the RBCs for its
protection from being denatured in the plasma
and to prevent its loss through excretion via
the kidneys.

Answer 3

Hemoglobin

Question 4

2 reasons why Hemoglobin is located inside
the RBCs

Answer 4

1. For its protection from denaturation,
   particularly in the plasma.
2. To prevent its loss through excretion via the
   kidneys

Question 5

Hemoglobin in RBC:

Answer 5

approx. 34 g/dL

Question 6

Cytoplasmic content of RBCs:

Answer 6

approx. 95%

Question 7

MW of Hgb

Answer 7

64,000 Daltons

Question 8

Total body weight = ____ ang weight ng Hgb

Answer 8

1%

Question 9

Functions of Hemoglobin

Answer 9

1) Transports oxygen from lungs to tissues
2) Transports carbon dioxide from tissues to the
lungs
3) Transports of nitric oxide
4) Contributes to acid-base balance

Question 10

2 additional functions of Hgb

Answer 10

1. Transportation of Nitric Oxide
2. Contributes to acid-base balance

Question 11

Nitric oxide is a vasodilator and a substance that
causes the dilation of blood vessels.

Answer 11

Transportation of Nitric Oxide

Question 12

The Hgb molecule is considered as a globular protein. This
globular protein is composed of _____

Answer 12

2 different pairs of
polypeptide chains

Question 13

the Hgb molecule is also composed of _____ heme groups.

Answer 13

4

Question 14

(True or False)
Each heme group is
embedded in each of the 4 polypeptide chains.

Answer 14

True

Question 15

Aside from iron and protoporphyrin 9
and other polypeptide chains, what is/are the additional structures of heme group?

Answer 15

2,3 BPG or 2,3 Bisphosphoglyceric Acid

Question 16

SUMMARY OF COMP. OF HEME GROUPS:

Answer 16

1. Iron
2. Protoporphyrin IX
3. Polypeptide chains
4. 2,3Bisphosphoglyceric Acid (BPG)

Question 17

Consists of: Protoporphyrin IX (ring of carbon, hydrogen and nitrogen atoms) + Ferrous Iron (Fe2+)

Answer 17

Heme/Ferroprotoporphyrin IX

Question 18

Considered as the protein portion of the Hgb because
it is made up of amino acids which are building blocks
of protein molecules

Answer 18

Globin Chains

Question 18

Consists of 2 identical pairs of unlike polypeptide
chains

Answer 18

Globin Chains

Question 19

gives rise to
different types of globin chains

Answer 19

Variation in amino acid sequence

Question 20

divided into 8 helices (linear &
rigid) separated by 7 non helical segments
(flexible)

Answer 20

1 globin chain

Question 21

(Hemoglobin Molecule)
Primary Structure

Answer 21

amino acid sequence of the
polypeptide chains

Question 22

(Hemoglobin Molecule)
Secondary Structure

Answer 22

chain arrangements in helices
and nonhelices

Question 23

(Hemoglobin Molecule)
Tertiary Structure

Answer 23

arrangement of the helices into
pretzel- like configuration | heme → suspended
between E & F helices

Question 24

(Hemoglobin Molecule) Quarternary Structure/Tetramer

Answer 24

complete hemoglobin molecule | spherical/globular | 4 heme groups + 4 globin chains

Question 25

(HEME GROUPS) ● Inside the cleft pocket; the amino acids there are ____

Answer 25

HYDROPHOBIC

Question 26

(HEME GROUPS) ● Amino acids outside the cleft are considered as

Answer 26

HYDROPHILIC

Question 27

predominant adult hemoglobin

Answer 27

HbA

Question 28

glycated hemoglobin (4% to 6%)

Answer 28

HbA1c

Question 29

non enzymatic binding of various sugars to the globin chain over the life span of the RBC

Answer 29

Glycation

Question 30

is the production of hgb, actually we cannot produce hgb if hindi muna magooccur ang heme synthesis & globin synthesis.

Answer 30

Hemoglobin biosynthesis

Question 31

occurs in the mitochondria and cytoplasm of BM erythroid precursor cells * Begins in basophilic normoblast (prorubricyte) |Ends in polychromatophilic erythrocyte

Answer 31

Hemoglobin synthesis

Question 32

There is two locations in the hgb synthesis:

Answer 32

1. MITOCHONDRION 2. CYTOPLASM (heme & globin meets)

Question 33

starts in the nucleus & onced the globin is produced in the ribosomes they are being released in the cytoplasm where heme & globin meet.

Answer 33

GLOBIN SYNTHESIS

Question 34

excess protoporphyrin in the mitochondrion

Answer 34

Free erythrocyte protoporphyrin (FEP)

Question 35

FEP complexed with zinc

Answer 35

Zinc Protoporphyrin (ZPP)

Question 36

found normally in the cytoplasm of the developing RBCs | represent storage form of iron that was not used in heme synthesis

Answer 36

Ferritin