Biochem Flashcards

0
Q

Why are the nucleolus and mitochondria so prominent in metabolically active cells?

A

Nucleolus- site of ribosome manufacture

Mitochondria- have own DNA and prot- site of respiration

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1
Q

What are the 3 proteins making up the cytoskeleton?

A

Micro filaments, intermediate and microtubules

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2
Q

What are the 3 types of cell junctions and their purpose?

A

Desmosomes- micro filament belts, protect vs shearing forces, anchorage

Tight junctions- form seals, make cells impermeable, limit protein movement in cm and leakage of substances between cells

Gap junctions- large prot channels, communication betw cells

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3
Q

What is interstitial fluid?

A

Fluid surrounding cells

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4
Q

What are the 4 types of ion channels

A

Ungated (leak)
Voltage-gated
Mechano-gated
Ligand-gated

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5
Q

What is the difference between primary active transport and secondary active transport?

A

Primary- carrier prot hydrolysed ATP and uses some of the e for transport
Secondary- used potential e stored by conc diff of ion (one ion trans up grad, the other down)

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6
Q

What are the two types of exocytosis?

A

Constitutive

Regulated

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7
Q

What are the 4 types of Endocytosis?

A

Pinocytosis
Receptor-mediated endocytosis
Transcytosis
Phagocytosis

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8
Q

What is the difference between autocrine and paracrine cells?

A

Autocrine- messenger acts on secretory cell itself

Paracrine- adjacent cells affected

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9
Q

What is a ligand?

A

A chem messenger than binds to prot mols in membrane, cystol or nucleus

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10
Q

What is the association constant?

A

When rates of association and dissociation are at equilibrium

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11
Q

What is down regulation?

A

Memb receptor number decrease in response to increased ligand conc
Removed from cm via receptor-mediated endocytosis
Therefore cells less sensitive to ligand when ligand levels high

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12
Q

What does adding a high energy phosphate group to a receptor and why does it happen?

A

Kinases phosphorylate protein and phosphorylase enzymes reverse process
Either desensitises or sensitises receptor (ie either decreases or increases affinity for ligand)

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13
Q

What is the action of tyrosine kinase?

A

It is activated on the cytoplasmic side of the membrane if a certain receptor is activated- then activated enzyme to phosphorylate tripsine to give yield to ATP and protein

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14
Q

What happens when an agonist bonds to a GPCR?

A

Activates g-protein- affinity for GTP increases (normally binds to GDP)- dissociates from receptor inside the cell-> can associate with other membrane-bound signal transduction molecules
GTP-ase activity inactivated and so re-associates with membrane receptor

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15
Q

What do tonic and antagonistic signals do?

A

Tonic- always there but varies in intensity

Antagonistic- uses diff signals to send physiological parameter in opp directions

16
Q

Give emailed of fibrous, globular and me rainouts proteins

A

Fibrous- collagen, keratin, actin
Globular- enzymes, antibodies
Membranous- channels, receptors

17
Q

How do enzymes increase the ror?

A

Exclude water
Brings substrates together
Stabilise transition state
Transfer chem groups

18
Q

What is the difference between isoteric and allosteric enzyme-substrate binding?

A

Isoteric- ror inc w substrate conc till enzyme saturated
Allosteric- substrate induces conformational change in enzyme via binding to allosterix site that either increases or decreases activity (sigmoidal curve)

19
Q

What are the effects of insulin?

A

Promotes glycogen storage in liver and muscle and inhibits gluconeogenesis
Promotes prot synthesis in liver and muscle and promotes fat storage in adipocytes

20
Q

What are ketone bodies?

A

They are what acetyl CoA is converted to if it doesn’t renter the TCA cycle (acetone, acetoacetate, D-3-hydroxy-butrate
Used in starvation mode as fuel

21
Q

What are the two types of amino acid breakdown?

A

Glycogenic

Ketogenic