Evidence that the two amino termini of plasma fibronectin are in close proximity: a fluorescence energy transfer study.

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Wolff C, Lai CS

Evidence that the two amino termini of plasma fibronectin are in close proximity: a fluorescence energy transfer study.

Biochemistry. 1988 May 3;27(9):3483-7.

PubMed ID

3390446 [ View in PubMed

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Abstract

A fluorescence energy transfer technique has been used to study the intramolecular distance between the two amino termini of human plasma fibronectin. The glutamine-3 residue near the amino terminus of each chain was labeled enzymatically with either monodansylcadaverine or monofluoresceinylcadaverine by use of coagulation factor XIIIa. The nonradiative fluorescence energy transfer between the dansyl (donor) and fluorescein (acceptor) pair in the same protein molecule was determined from steady-state fluorescence measurements. On the basis of the transfer efficiency of 78%, the intramolecular distance between two glutamine-3 residues of fibronectin was estimated to be approximately 23 A, suggesting that the two amino termini of plasma fibronectin are in close proximity. High salt, which affects the hydrodynamic properties of the protein, has no effect on the measured distance. The results support the contention that both compact (in low salt) and expanded (in high salt) conformers of fibronectin are relatively spherical in shape.

DrugBank Data that Cites this Article

Drug Enzymes

Drug	Enzyme	Kind	Organism	Pharmacological Action	Actions
L-Glutamine	Coagulation factor XIII A chain	Protein	Humans	Unknown	Substrate	Details