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• W2059893562 startingPage "161" @default.
• W2059893562 abstract "The β‐amyloid peptide (βA4), derived from a larger amyloid precursor protein, is the principal component of senile plaques in Alzheimer's disease. Here we report that the full‐length (1–40) synthetic βA4 peptide, containing one glutamine and two lysine residues, is able to form homopolymers in a transglutaminase‐mediated reaction. Moreover, transglutaminase catalysed the formation of heteropolymers in reactions of βA4 with α 2 M receptor, a constituent of amyloid plaques, and with extracellular matrix proteins. Incorporation of site‐specific probes followed by enzymatic digestion and sequencing of tracer‐containing fractions demonstrated that both Lys 16 , Lys 28 and Gin 15 in βA4 were susceptible to cross‐linking by transglutaminase." @default.
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• W2059893562 date "1994-01-31" @default.
• W2059893562 modified "2023-10-17" @default.
• W2059893562 title "Identification of glutamine and lysine residues in Alzheimer amyloid βA4 peptide responsible for transglutaminase-catalysed homopolymerization and cross-linking to α₂M receptor" @default.
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• W2059893562 doi "https://doi.org/10.1016/0014-5793(94)80356-0" @default.
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