Membrane transport Flashcards
1
Q
GLUT1
A
- 12 transmembrane Ahelices
- moves glucose with its gradient. Either direction
1. Outward open conf binds glucose. Dependant on Km and concentration
2. Ligand-bound occluded
3. Inward open release of glucose
4. Ligand-free occluded
2
Q
ATP powered pumps
A
- P class: H+ and salt ion. Ion gradients. Phosphoprotein intermediate
- V/F classes: H+ ions
- ABC superfamily: toxins, drugs, phospholipids, proteins
3
Q
Ca+2 ATPase in Sarco Reticulum
A
- P pump
- establish low resting Ca+2 (10-7) in cytosol of most cells
- muscle relaxation = Ca+2 from cytosol –> SR
- 2 conformations
E1: cytosolic face
E2: exoplasmic (ER lumen) face - 1 ATP for 2 Ca+2
4
Q
Ca+2 ATPase steps
A
- 2Ca+2 and 1 ATP bind. E1
- Hydrolysis + phosphorylation= conf change. E2. ADP release
- Ca released into lumen
- Dephosphorylation. Pi released. E1
5
Q
Na/K pump
A
- 3 Na out and 2 K in per ATP
- each ion moves against its gradient
- E1 conf: dephosp opens to cytosolic face (Na associates, K dissociates)
- E2: phos opens to exoplasmic face (Na dissociates, K associates)
6
Q
Na/K steps
A
- Na and ATP bind. E1
- Phos of aspartate, ADP released. E2
- Na release and K binds. E2
- Dephos. E1
- K release. E1
7
Q
Multi-Drug Resistant Transporter (ABCB1)
A
- ABC superfamily. drugs,toxins, hydrophobic/philic
- 2 Transmembrane (T) and cytosolic ATP-binding domains (A)
- ATP hydrolysis= solute movement
- Ligand-binding cavity alternately exposed to exoplasmic/cytoplasmic faces
- high expression in liver
8
Q
Non-Gated Ion channels and Resting potential
A
a) impermeable to Cl, K, Na
- no electric potential
- osmotic potential is the same on either side of cell
- composition is different
b) only permeable to K
- potential = -59mV. Cytosolic face is negative (inside)
- K moves from cytosol to exoplasmic
9
Q
Animal cell resting potential
A
- generated by Na/K ATPase and non-gated K channels
- -70mV
- flutuates in axons/neurons. Dopolarization
10
Q
K+ channels
A
- tetramers of 4 identical subunits
- selectivity filter due to backbone of carbonyl oxygens of amino acids
- K fits perfectly, bound to oxygens
- Na imperfect fit, higher in energy. thermodynamically more stable for it to stay hydrated outside of channel
- Na/K are hydrated in solution, K dehydrated in channel pore
11
Q
2-Na/1-glucose symporter
A
- cotransporter: both symporter and antiporter
- electrochemical gradient
- 2 Na and 1 glucose outside –> inside
- against glucose gradient
- with Na gradient
12
Q
2-Na/1-glucose symporter steps
A
- 2 Na and glu bind outward conf
- conf change. occluded substrates
- conf change, inward facing
- dissociation of substrates
- revert to outward facing