Abstract
During the last two decades a great effort to understand the structure of apolipoprotein B (apoB) has been made, however despite the relative ease of isolation, the detailed physico-chemical characteristics of this protein are still unknown due to its large apparent molecular weight and insolubility in aqueous buffers after delipidation. The function of apoB is only partially known. In LDL. apoB is the predominant apolipoprotein and is the protein ligand for binding to the high affinity LDL receptor1. Genetic absence of apoB is associated to severely impaired lipid transport2. In addition, it is now known that there are multiple iorms of apoB with different molecular weights in the rat3–5 and in man6. In man there are two major forms, the larger apolipoprotein being designated apoB-100 and the small one apoB-486–8. ApoB-100 is of hepatic origin and is present on VLDL, IDL, and LDL. ApoB-48 is of intestinal origin and is found predominantly on chylomicrons and on chylomicrons remnants within VLDL and IDL6–8.
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© 1986 Springer Science+Business Media New York
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Gabelli, C., Gregg, R.E., Brewer, H.B. (1986). Immunoblot Analysis of the Different Apolipoprotein B Species. In: Sirtori, C.R., Nichols, A.V., Franceschini, G. (eds) Human Apolipoprotein Mutants. NATO ASI Series, vol 112. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9474-1_21
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DOI: https://doi.org/10.1007/978-1-4615-9474-1_21
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