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. 1998 Jul;72(7):5937–5947. doi: 10.1128/jvi.72.7.5937-5947.1998

TABLE 2.

Kinetic and affinity values for gDt-HveAt complex formation

Immobi- lized ligand Analyte kon (103 s−1 M−1) koff (10−2 s−1) KD (10−6 M)e
HveAt gD1 (306t)a 6.1 ± 0.6d 2.0 ± 0.2 3.2 ± 0.6
HveAt gD1 (Δ290-299t)a 240 ± 70 0.78 ± 0.1 0.033 ± 0.01
HveAt gD2 (306t)a 8.3 1.2 1.5
HveAt gD1 (QAAt)a 6.4 1.1 1.8
HveAt gD1 (∇34t)b Does not bind
HveAt gD1 (∇126t)b 1.2 2.6 22
HveAt gD1 (∇243t)b 11 1.5 1.3
HveAt gD1 (cys1,5)b 2.9 1.6 5.4
HveAt gD1 (cys2,6)b 2.2 2.4 11
HveAt gD1 (cys3,4)b 1.1 1.7 16
gD1 (306t) HveAtc 7.1 1.7 2.3
gD1 (Δ290299t) HveAt Data do not fit
a

Concentrations for data analysis were calculated by assuming that gDt is a dimer in solution and by using twice the mass spectrometry values for molecular mass (Table 1). 

b

Concentrations were calculated as described in footnote a with the mass spectrometry values for gD1 (306t). Small differences in amino acid composition do not affect concentration calculations significantly. 

c

Concentrations for data analysis were calculated by assuming that HveAt is a dimer in solution and by using twice the mass spectrometry values for molecular mass (50). 

d

Such values are means ± the standard deviations of results from at least three separate experiments. 

e

Chi-square values for the global fits ranged from 0.93 to 3.74.