TABLE 1. Changes in tryptophan and TNS fluorescence obtained by LAH, HAH and normal pentasaccharide binding to native, latent and cleaved antithrombin (AT).

The changes in tryptophan fluorescence were obtained from the ΔFmax values derived from computer-fits of stoichiometric titration data to the equilibrium binding equation. The changes in TNS fluorescence were obtained from emission spectra recorded at λ_ex 326 nm, as described in Experimental Procedures. The negative changes in TNS fluorescence values at λ_em 455 nm are reported

		Fluorescence change (%)
AT form	Fluorescence form	Normal pentasaccharide	HAH	LAH
Native	Tryptophan	40	43	8
	TNS	28	51	0
Latent	Tryptophan	6	6	2
	TNS	24	32	0
Cleaved	Tryptophan	3	3	<1
	TNS	66	51	0