Human brain peptidase activity with the specificity to generate the N-terminus of the Alzheimer β-amyloid protein from its precursor
Autor: | J. A. Biggins, J.R. McDermott, A.M. Gibson |
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Rok vydání: | 1992 |
Předmět: |
Molecular Sequence Data
Biophysics Peptide Cleavage (embryo) Biochemistry Substrate Specificity Amyloid beta-Protein Precursor Alzheimer Disease Endopeptidases medicine Amyloid precursor protein Humans Amino Acid Sequence Molecular Biology Peptide sequence Cerebral Cortex chemistry.chemical_classification Amyloid beta-Peptides biology Cell Biology Human brain medicine.disease N-terminus medicine.anatomical_structure chemistry biology.protein Metalloendopeptidase Alzheimer's disease Peptides |
Zdroj: | Biochemical and Biophysical Research Communications. 185:746-752 |
ISSN: | 0006-291X |
DOI: | 10.1016/0006-291x(92)91689-n |
Popis: | The synthetic peptide acetyl-Glu-Val-Lys-Met-Asp-Ala-Glu-Phe-NH2, which spans the cleavage site (Met-Asp) required to generate the N-terminus of the Alzheimer beta-amyloid protein from its precursor, was used to search for human brain peptidases which may be involved in this potentially amyloidogenic process. In both soluble and particulate fractions from human brain the primary cleavage point of the peptide was the Met-Asp bond. Purification and characterization of the activity from the soluble fraction showed that it was metalloendopeptidase 24.15 (EC3.4.24.15). This enzyme is therefore a candidate for the generation of the N-terminus of beta-amyloid protein from its precursor. |
Databáze: | OpenAIRE |
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