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• W2017395439 abstract "Microfibrils were extracted from human amnion in the form of a beaded filament and analyzed for the presence of transglutaminase-derived cross-links using acrylonitrile derivatization. The cross-link structure was isolated from protease hydrolysates of beaded filaments and identified as a phenylthiocarbamyl amino acid derivative by comparison to a standard. Acid hydrolysis of the isolated cross-link gave the expected lysine and glutamic acid in a 1:1 ratio. The beaded filaments were also treated with trypsin to produce a fraction that contained the bead structure and a fraction containing fragments of the interbead filaments. Cross-links were detected in the interbead filaments but not in the beads. A large tryptic peptide that contained a cross-link was isolated and sequenced. The two amino acid sequences obtained identified both of the cross-linked molecules as fibrillin-1 and enabled the approximate localization of the cross-link sites within the molecule. The locations of cross-link sites on two adjacent molecules fixed the relative positions of fibrillin monomers within the microfibrils, providing insight into the spatial organization of fibrillin within the elastic microfibrils." @default.
• W2017395439 created "2016-06-24" @default.
• W2017395439 creator A5023915258 @default.
• W2017395439 creator A5044813451 @default.
• W2017395439 date "1997-12-01" @default.
• W2017395439 modified "2023-09-25" @default.
• W2017395439 title "Alignment of Fibrillin Molecules in Elastic Microfibrils Is Defined by Transglutaminase-Derived Cross-Links" @default.
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• W2017395439 doi "https://doi.org/10.1021/bi971036f" @default.
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