Journal
FRESENIUS JOURNAL OF ANALYTICAL CHEMISTRY
Volume 366, Issue 8, Pages 869-872Publisher
SPRINGER VERLAG
DOI: 10.1007/s002160051587
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Theophylline (Th) has been selectively conjugated to the four amino groups of melittin (Mel) by solid phase peptide synthesis. The cytolytic activity of the resultant Th-Mel compounds was tested on liposomes trapping the bovine serum albumin (BSA) conjugate with 4,7-bis(chlorosulfophenyl)- 1,10-phenanthroline-2,9-dicarboxylic acid (BCPDA). The loss of lytic activity was the highest for Th-K-7-Mel. Th-G(1)-Mel retains almost the same lyric activity as Mel. A homogeneous liposome time-resolved fluoroimmunoassay (LITRFIA) of Th in serum has been carried out with Th-G(1)-Mel between 5 ng and 10 mu g.
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