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Synthesis of tritium‐labelled β‐amyloid fragments
Author(s) -
Gulyás Éva C.,
Soós Katalin,
Varga Jószef,
Tóth Géza,
Penke Botond
Publication year - 1998
Publication title -
journal of labelled compounds and radiopharmaceuticals
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.432
H-Index - 47
eISSN - 1099-1344
pISSN - 0362-4803
DOI - 10.1002/(sici)1099-1344(1998080)41:8<763::aid-jlcr122>3.0.co;2-r
Subject(s) - chemistry , tritium , labelling , peptide , residue (chemistry) , high performance liquid chromatography , specific activity , amyloid (mycology) , hydrolysis , chromatography , radiochemistry , biochemistry , enzyme , inorganic chemistry , physics , nuclear physics
Two fragments of β‐amyloid(1–42) peptide, β‐amyloid(31–35) and β‐amyloid(25–35), were synthesized and labelled with tritium in the Leu 34 residue. Precursor peptides containing ΔLeu 34 were prepared by solid phase peptide synthesis using manual Fmoc strategy. Tritium labelling was carried out by catalytic saturation, yielding [ 3 H‐Leu 34 ]β‐amyloid(31–35) and [ 3 H‐Leu 34 ]β‐amyloid(25–35) with very high specific activities of around TBq/mmol (120 Ci/mmol). The labelling peptides were investigated by RP‐HPLC and the distribution of the tritium was determined by acidic hydrolysis followed by RP‐HPLC analysis. © 1998 John Wiley & Sons, Ltd.