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Linke, R.P. ; Bommer, J. ; Ritz, E.R. ; Waldherr, R. ; Eulitz, M.

Amyloid kidney stone of uremic patients consist of Beta2-microglobulin fragments.

Biochem. Biophys. Res. Commun. 136, 665-671 (1986)
DOI
Open Access Green as soon as Postprint is submitted to ZB.
Urinary stones with amyloid structure, obtained from uremic patients, were analyzed according to molecular weight, amino acid sequence, and antigenic content. A major protein of approximately 7 kD, designated AB protein, was isolated by size exclusion using HPLC in 60% formic acid. AB protein reacted in immunodiffusion only with an antiserum to β2-microglobulin, with β2m spurring over AB protein. N-terminal amino acid sequence analysis defined two fragments homologous to β2m. One fragment commenced with Ile at position 7 and the other with Ser at position 20, with a cleavage point subsequent to a lysyl residue in both. It is concluded that β2m is a precursor of urinary amyloid stones and intratubular concretions of patients with preterminal and terminal renal failure; limited proteolysis is involved in AB amyloid generation.
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Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
ISSN (print) / ISBN 0006-291X
e-ISSN 1090-2104
Journal Biochemical and Biophysical Research Communications
Quellenangaben Volume: 136, Issue: 2, Pages: 665-671 Article Number: , Supplement: ,
Publisher Elsevier
Non-patent literature Publications
Reviewing status Peer reviewed
Institute(s) Institut für Immunologie