GLOBULAR PROTEINS Flashcards

1
Q

Group of specialized proteins that contain heme as a tightly bound prosthetic group.

A

GLOBULAR HEMEPROTEINS

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2
Q

a hemeprotein present in heart and skeletal muscle functions both as a reservoir for oxygen and as an oxygen carrier that increases the rate of transport of oxygen within the muscle cell.

A

Myoglobin

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3
Q

STRUCTURE OF HEME

A

protoporphyrin IX and ferrous iron (Fe2+)

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4
Q

the major hemoglobin in adults, is composed of four polypeptide chains (two 𝛂 chains and two ꞵ chains) held together by noncovalent interactions.

A

Hemoglobin A,

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5
Q

is the arrangement of multiple protein subunits into a functional unit.
highest level of protein structure.

A

QUATERNARY STRUCTURE OF HEMOGLOBIN

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6
Q

This protein carries oxygen in the blood. It is made up of four subunits, two each of the alpha and beta types.

A

Hemoglobin

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7
Q

This enzyme synthesizes new strands of DNA. It is made up of ten subunits.

A

DNA polymerase:

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8
Q

These organelles are responsible for protein synthesis. They are made up of multiple protein subunits and RNA molecules.

A

Ribosomes

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9
Q

These proteins help the body fight infection. They are made up of two identical heavy chains and two identical light chains

A

Antibodies

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10
Q

is a plot of Y measured at different partial pressures of oxygen (pO2).

A

Oxygen-dissociation curve:

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11
Q

are changes in the activity of a protein caused by the binding of a molecule to a site other than the active site.

A

ALLOSTERIC EFFECT

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12
Q

responsible for the cooperative binding of oxygen.

A

Heme–heme interactions:

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13
Q

phenomenon where the affinity of HgB to oxygen is inversely related to the concentration of co2

A

bohr effect

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14
Q

is an important regulator of the binding of oxygen to hemoglobin.

is synthesized from an intermediate of the glycolytic pathway.

A

2,3- Bisphosphoglycerate (2,3-BPG)

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15
Q

indicates that hemoglobin has a higher affinity for oxygen.

A

shift to the left

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16
Q

indicates that hemoglobin has a lower affinity for oxygen

A

shift to the right i

17
Q

is normally synthesized only during fetal development.

is a tetramer consisting of two α chains plus two γ chains (α2γ2).

A

Fetal hemoglobin (HbF)

18
Q

are synthesized in the adult, although at low levels compared with HbA.

: is a minor component of normal adult hemoglobin, first appearing shortly before birth and, ultimately, constituting about 2% of the total hemoglobin. It is composed of two α-globin chains and two δ-globin chains (α2δ2)

A

Hemoglobin A2:

19
Q

is the most abundant form of glycosylated hemoglobin. Increased amounts of HbA1c are found in RBC of patients with diabetes mellitus,

A

Hemoglobin A1c

20
Q

oftebn caused by vit. 12 deficiency

A

megaloblastic anemia