Human Brain βA4 Amyloid Protein Precursor of Alzheimer's Disease: Purification and Partial Characterization
作者： Robert D. Moir , Ralph N. Martins , Ashley I. Bush , David H. Small , Elizabeth A. Milward
DOI: 10.1111/J.1471-4159.1992.TB08465.X
关键词: Alzheimer's disease 、 Immunoprecipitation 、 Human brain 、 Membrane protein 、 Amyloid precursor protein 、 P3 peptide 、 Proteolysis 、 Autolysis (biology) 、 Biology 、 Biochemistry
摘要: The major component of the amyloid deposition that characterizes Alzheimer's disease is 4-kDa βA4 protein, which derived from a much larger protein precursor (APP). A procedure for complete purification APP human brain described. same amino terminal sequence was found in two patients with and one control subject. Two forms were identified apparent molecular masses 100–110 kDa 120–130 kDa. Soluble membrane fractions contained nearly equal amounts both humans rats. Immunoprecipitation carboxyl terminus-directed antibodies indicates soluble are truncated. Carboxyl terminus truncation membrane-associated also to occur during postmortem autolysis. availability purified will facilitate investigation its normal function events lead abnormal cleavage disease.
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