The tryptophan fluorescence of Tetracarbidium conophorum agglutinin II and a solution-based assay for the binding of a biantennary glycopeptide.

摘要: The plant lectin Tetracarbidium conophorum agglutinin II binds to glycoproteins and glycopeptides in a structurally specific manner [Animashaun et al., (1994) Glycoconjugate J.11, 299–303]. We have characterized the steady-state time-resolved fluorescence of tryptophan residues this lectin. (λex = 295 nm, λem 350 nm) decay is complex can be described by four times with following values: τ1 7.4nsec, α1 0.22; τ2 2.9 nsec, α2 0.25; τ3 l.0 α3 0.34; τ4 0.2 α4 0.18. addition biantennary glycopeptide \(\begin{array}{*{20}c} {Gal\beta (1 \to 4)GlcNAc\beta 2)Man\alpha 6)\neg } \\ {Man\beta 4)GlcNAC\beta 4)GlcAc\beta )\begin{array}{*{20}c} {Glu - Nh_2 | {Asn} {COOH} \end{array} 3)} \) results quench an 8 nm blue shift emission spectrum. effect saturable, association constant 1.8×105 M−1. may therefore utilized characterize thermodynamically binding interactions between glycoprotein.