Oxygen Transporters And Protein Secretion Flashcards

1
Q

How is the harm group bound to the polypeptide chain?

A

Histidine residue

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2
Q

What type of dependence des oxygen binding to myoglobin show and what does his imply?

A

Hyperbolic

Constant affinity for oxygen

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3
Q

What type of curve dos oxygen binding in haemoglobin show?

What does this imply

A

Sigmoidal binding curve

This implies that the affinity for oxygen. Increases with the partial pressure for oxygen

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4
Q

What ensure oxygen transport by haemoglobin?

A

Coopertaivity enhances it as the binding of oxygen promotes the transistion from a low affinity -T state to a high affinity r state

Haemoglobin has a high affinity for oxygen i. The lungs and a low afffinity in the tissues

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5
Q

How does BPG regulate oxygen binding

A

It is an allosteric effector

It lowers the affinity of Hb for oxygen so stabilises the T state

Shifts curve to right

BPG interacts wit positively charged reissues on beta units

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6
Q

How does CO2 act as a allosteric effector

A

Binding of CO2 nd H+ lowers the affinity

Stabilises t state

Allows delivery of oxygen at metabolically active tissues that produce CO2 and H+

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7
Q

How is carbon monoxide regulate oxygen binding

A

It binds to haemoglobin 250x more regularly than O2

Blocks further oxygen binding

Stabilises R state in unaffected subunits which prevents dissociation at tissues

Shits curve to the left meaning they are less likely to dissociate

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8
Q

What causes sickle cells disease

A

Mutation of glutamate to valine in beta haem group

Haemoglobin stick together and aggregate

Valine residue lies on the surface in the t state

This causes the cells to be more prone to lose- anaemia

More rigid- block microvasculatue

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9
Q

How are proteins destined for the cytosol or post translational import into organless synthesised?

A

Free ribosomes

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10
Q

How are proteins destined for membranes or secretory pathways via co-translational insertion synthesised by?

A

Synthesised by ribosomes on the RER

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11
Q

What is constiuitive secretion?

A

Secreted with no regulation

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12
Q

What is regulated secretion?

A

Controlled
E.g.
endocrine cells- secreting hormones
Exocrine cells- secreting digestive juices
Neurocrine cells- secreting neurotransmitters

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13
Q

What does the pre part of a protein represent?

A

Defines the signal sequence which is removed during processing

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14
Q

What are the functions of the endoplasmic reticulum?

A
. Insertion of proteins into membranes
 • Specific proteolytic cleavage
 • Glycosylation 
• Formation of S-S bonds 
• Proper folding of proteins
 • Assembly of multisubunit proteins 
• Hydroxylation of selected Lys and Pro residues
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15
Q

Where does posttranslational modifiction occur?

A

Endoplasmic reticulum

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16
Q

Function of Golgi apparatus

A

Movement of proteins to the cis-Golgi through budding

• Further protein modifications

• Release through trans-Golgi
to membrane/organelles

17
Q

What produces collagen?

A

Fibroblasts

18
Q

Structure of collagen

A

Basic unit- tropocollagen

Collagen is formed of thee polypeptide chains that form a right handed helix structure

The triple helical structure allows strength

H bonds between polypeptide chains

Every third amino acid is glycine

19
Q

What causes scurvy?

A

Enzyme prolyl hydroxylase requires vitamin C and fe2+ ions for its activity to catalyse the hydroxylation of proline and lysine residues.

Vitamin C deficiency causes reduced activity of the enzyme which results in reduced stabilisation of the triple helical structure of collagen

Abnormal collagen leads to defective connective. Tissue

Leads to easy bruising tiredness irritability swollen and painful joints and swelled and bleeding gums