Processing of the pre-beta-amyloid protein by cathepsin D is enhanced by a familial Alzheimer's disease mutation.

Dreyer, R N; Bausch, K M; Fracasso, P; Hammond, L J; Wunderlich, D; Wirak, D O; Davis, G; Brini, C M; Buckholz, T M; König, G

Dreyer, R N; Bausch, K M; Fracasso, P; Hammond, L J; Wunderlich, D; Wirak, D O; Davis, G; Brini, C M; Buckholz, T M; König, G.

Affiliation

Dreyer RN; Institute for Molecular Biologicals, Miles Inc., Pharmaceuticals Division, West Haven, Connecticut 06516.

Eur J Biochem ; 224(2): 265-71, 1994 Sep 01.

Article in En | MEDLINE | ID: mdl-7523115

Subject(s)

Alzheimer Disease/genetics; Amyloid beta-Protein Precursor/genetics; Amyloid beta-Protein Precursor/metabolism; Cathepsin D/metabolism; Frontal Lobe/metabolism; Point Mutation; Protein Processing, Post-Translational; Alzheimer Disease/metabolism; Amino Acid Sequence; Amyloid beta-Protein Precursor/isolation & purification; Antibodies, Monoclonal; Chromatography, Ion Exchange; Dansyl Compounds; Electrophoresis, Polyacrylamide Gel; Epitopes/analysis; Humans; Hydrogen-Ion Concentration; Molecular Sequence Data; Peptide Fragments/analysis; Peptide Fragments/chemistry; Peptide Fragments/isolation & purification; Recombinant Proteins/metabolism; Substrate Specificity

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Collection: 01-internacional Database: MEDLINE Main subject: Protein Processing, Post-Translational / Cathepsin D / Amyloid beta-Protein Precursor / Point Mutation / Alzheimer Disease / Frontal Lobe Limits: Humans Language: En Journal: Eur J Biochem Year: 1994 Document type: Article

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