Determination of amyloid β protein precursors harboring active form of proteinase inhibitor domains in cerebrospinal fluid of Alzheimer's disease patients by trypsin-antibody sandwich ELISA

β-Amyloid protein precursors (APP) having proteinase inhibitor domains (APPI) were quantified by a new sandwich enzyme linked immunosorbent assay for detection of active (free) form of proteinase inhibitors by using trypsin in place of the first antibody and by denaturation of APPI-trypsin complex i...

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Veröffentlicht in:	Biochemical and biophysical research communications 1990-02, Vol.166 (3), p.1453-1459
Hauptverfasser:	Kitaguchi, Nobuya, Tokushima, Yasuo, Oishi, Kiyomi, Takahashi, Yasuyuki, Shiojiri, Satoshi, Nakamura, Shigenobu, Tanaka, Seigo, Kodaira, Ryoji, Ito, Hirataka
Format:	Artikel
Sprache:	eng
Schlagworte:	Alzheimer Disease - cerebrospinal fluid Alzheimer's disease Amino Acid Sequence amyloid Amyloid - cerebrospinal fluid Amyloid beta-Protein Precursor Analytical, structural and metabolic biochemistry Biological and medical sciences cerebrospinal fluid Enzyme-Linked Immunosorbent Assay Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Humans Hydrolases Indicators and Reagents man Molecular Sequence Data Molecular Weight Protease Inhibitors - cerebrospinal fluid Protein Binding Protein Precursors - cerebrospinal fluid proteinase Sequence Homology, Nucleic Acid Trypsin - metabolism
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Zusammenfassung:	β-Amyloid protein precursors (APP) having proteinase inhibitor domains (APPI) were quantified by a new sandwich enzyme linked immunosorbent assay for detection of active (free) form of proteinase inhibitors by using trypsin in place of the first antibody and by denaturation of APPI-trypsin complex in the microtiterplate. The concentration of APPs having APPI in cerebrospinal fluid of Alzheimer's disease patients was found, by this method, to be significantly elevated compared with those of multi-infarct dementia.
ISSN:	0006-291X 1090-2104
DOI:	10.1016/0006-291X(90)91030-V