MYOGLOBIN AND HEMOGLOBIN Flashcards

(40 cards)

1
Q

n iron-containing cyclic

tetrapyrrole linked by methyne bridges

A

heme

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2
Q

resides at the center of the planar tetrapyrrole.

ferrous or ferric

A
ferrous iron (Fe
2+)
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3
Q

proteins with metal-containing tetrapyrrole prosthetic groups

A

cytochromes (Fe and Cu) and chlorophyll (Mg)

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4
Q

Angle of bond that links the O2 and myoglobin

A

121

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5
Q

Angle that separates the 2 atoms of oxygen and electrons that are coplanar

(Left)

A

120

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6
Q

Separates the pairs of electron and triple bonds that are arranged in linear fashion

(Right)

A

180•

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7
Q

The oxygen-binding curve for myoglobin

A

Hyperbolic

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8
Q

Load O2 readily at PO2 of lung capillary bed (100mmHg)

Myoglobin or hemoglobin?

A

Myoglobin

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9
Q

Amount of Bound O2 at PO2 released in active muscle

A

20mmHg (capillary; active muscle)

40mmHg (other tissues; mixed venous O2 tension)

100mmHg (arterial)

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10
Q

mmHg of of PO2 released during strenous exercise

A

5 mmHg (required for cytochrome oxidase)

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11
Q

(HbA; normal adult hemoglobin)

A

α2β2

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12
Q

(HbF; fetal hemoglobin)

A

α2γ2

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13
Q

α2βS2

A

(HbS; sickle cell hemoglobin)

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14
Q

HbA2
; a minor adult
hemoglobin

A

α2δ2

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15
Q

hemoglobin to maximize both the
quantity of O2
loaded at the PO2 of the lungs

A

cooperative

binding

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16
Q

values of P50
for HbA and
HbF are 26 and 20 mm Hg

A

P50

-partial pressure of O2

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17
Q

a hemoglobin that carries CO2 to venous blood

18
Q

formed in erythrocytes by the hydration of CO2
to carbonic acid (H2CO3)

cabonate or bicarbonate ?

19
Q

changes the charge of amino terminal

20
Q

coupling of the interconversion of CO2 and H2CO3

21
Q

drives the conversion of bicarbonate to carbonic acid

His 146 or His 147 ?

22
Q
stabilizes deoxygenated (Tstate) hemoglobin by forming additional salt bridges that must be broken
prior to conversion to the R state.
23
Q

A mutation that compromise biologic function

HEMOGLOBINOPATHY or thalassemia?

A

hemoglobinopathy

24
Q

the heme iron is ferric rather than ferrous

methemoglobinemia or hemoglobinuria

A

methemoglobinemia

25
tissue hypoxia with increased RBC
polycythemia
26
nonpolar amino acid valine has replaced the polar surface | residue Glu6 of the β subunit
Hemoglobin S "STICKY PATCH" Hb A also provides sticky patch
27
Treatment for sickle cell disease
Inducing HbF expression to inhibit the | polymerization of HbS,
28
myoglobin released in urine following myocardial infarction
myoglobinuria
29
the partial or total absence of one or more α or β chains of hemoglobin myoglobinuria or thalassemia ?
Thalassemias
30
remains in blood for 6-8weeks. for DM
GLYCATED HEMOGLOBIN (HbA1c)
31
a consequence of cooperative interactions in the tetramer sigmoid or myoglobin
Sigmoidal hemoglobin
32
organic molecules that contain four five-membered heterocyclic (pyrrole) rings, linked in a cyclic or linear array. TETRAPYRROLES or trigly
TETRAPYRROLES
33
One binding of O2 in one subunit permits successive and easier binding of O2 for other subunits
ALLOSTERIC EFFECT
34
affinity of Hb for H+ and CO2 is affected by | changes in Hb-O2 saturation
HALDANE EFFECT
35
Dec. O2 and pH, Inc. CO2
Bohr effect
36
Dec. O2 and pH, Inc. CO2
Bohr effect "tissue"
37
Dec. CO2, INC. O2 and pH
Haldane effect | "lungs"
38
Caused by the uptake of O2 in the lungs.
Haldane Effect
39
His F8 is replaced by tyrosine | Forms a tight ionic complex that stabilizes Fe3+ state
Hemoglobin M
40
an odorless, colorless gas, which can cause sudden illness and death, is produced any time a fossil fuel is burned. CO gas is readily absorbed and is unchanged by the lungs
CARBON MONOXIDE