(a) WHY does it make sense that a receptor on the liver that recognizes and clea
ID: 64337 • Letter: #
Question
(a) WHY does it make sense that a receptor on the liver that recognizes and clears circulating glycoproteins would recognize an asialoglycoprotein moiety ???
(b) Why might one vaccine against HIV that is directed against an epitope on gp120 on the viral coat not block the binding of ALL HIV strains to host immune cells with functional CD4+ and CXCR5 receptors on their cell surface?
(c) If you were to use an antibody to identify a N-acetylglucosamine ( GlCNAC) transferase in a cell, what compartment of the cell would you expect to find this enzyme? Why?
(d) What might be the morphological consequence, at the level of a single cell, of a mutation in H1 histone that destabilizes its interactions with DNA? Why?
Explanation / Answer
a. It is because of the same carbohydrate moiety at receptors. the asialoglycoprotein receptor (ASGR) is capable of clearing glycoproteins bearing terminal Sia2,6GalNAc as well as ones bearing terminal Gal/ GalNAc and that the Mannose/GalNAc-4-SO4 receptor (MR) is capable of clearing glycoproteins bearing terminal GalNAc-4-SO4.
b. The The X5 antibody binds to a unique epitope on gp120 that is induced by interaction between gp120 and the receptor CD4 and enhaced by the coreceptor CCR. It shows strong activity at very low levels. This is why it does not block other and remains active.
c.They are mostly found in the lysosome. GlcNAc-1-phosphotransferase helps prepare certain newly made enzymes for transport to lysosomes. Lysosomes are compartments within the cell that use digestive enzymes called hydrolases to break down large molecules into smaller ones that can be reused by cells.
d.. It is because Histone H1 plays a crucial role in stabilizing higher order chromatin structure.Mutation cause the dephosphorylation of the chromatin which leads to the destabilisation of the chromatin fibre.
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