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Human brain beta-A4 amyloid protein precursor of Alzheimer's disease: purification and partial characterization.


Moir, RD and Martins, RN and Small, DH and Bush, AI and Milward, EA and Multhaup, G and Beyreuther, K and Masters, CL, Human brain beta-A4 amyloid protein precursor of Alzheimer's disease: purification and partial characterization. , Journal of Neurochemistry, 59, (4) pp. 1490-1498. ISSN 0022-3042 (1992) [Refereed Article]

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DOI: doi:10.1111/j.1471-4159.1992.tb08465.x


The major component of the amyloid deposition that characterizes Alzheimer's disease is the 4-kDa βA4 protein, which is derived from a much larger amyloid protein precursor (APP). A procedure for the complete purification of APP from human brain is described. The same amino terminal sequence of APP was found in two patients with Alzheimer's disease and one control subject. Two major forms of APP were identified in human brain with apparent molecular masses of 100110 kDa and 120130 kDa. Soluble and membrane fractions of brain contained nearly equal amounts of APP in both humans and rats. Immunoprecipitation with carboxyl terminus-directed antibodies indicates that the soluble forms of APP are truncated. Carboxyl terminus truncation of membrane-associated forms of human brain APP was also found to occur during postmortem autolysis. The availability of purified human brain APP will facilitate the investigation of its normal function and the events that lead to its abnormal cleavage in patients with Alzheimer's disease.

Item Details

Item Type:Refereed Article
Keywords: Amyloid protein precursor; βA4 amyloid; Alzheimer's disease; Postmortem degradation; Protein sequence; Proteolysis; Membrane protein
Research Division:Biomedical and Clinical Sciences
Research Group:Neurosciences
Research Field:Neurosciences not elsewhere classified
Objective Division:Health
Objective Group:Clinical health
Objective Field:Clinical health not elsewhere classified
UTAS Author:Small, DH (Professor David Small)
ID Code:75434
Year Published:1992
Web of Science® Times Cited:54
Deposited By:Research Division
Deposited On:2012-01-30
Last Modified:2012-04-04

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