Abstract:
:Cerebral deposits of beta/A4 amyloid protein is a pathologic sign of Alzheimer's disease. A synthetic partial-length (1-28) peptide of this protein contains one glutamine and two lysine residues. Here we show that this peptide can be a substrate of transglutaminase, which catalyzes cross-linking between glutamine and lysine residues in peptides, by demonstrating the formation of multimeric peptides due to the action of this enzyme. A modified (Lys28 to L-norleucine) version of the synthetic peptide was also cross-linked, but another modified version (Lys16 to L-norleucine) was very poorly cross-linked, indicating that Lys16 is involved exclusively in the cross-linking of the partial-length peptide catalyzed by transglutaminase.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Ikura K,Takahata K,Sasaki Rdoi
10.1016/0014-5793(93)81772-rsubject
Has Abstractpub_date
1993-07-12 00:00:00pages
109-11issue
1-3eissn
0014-5793issn
1873-3468pii
0014-5793(93)81772-Rjournal_volume
326pub_type
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