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. Author manuscript; available in PMC: 2011 Oct 15.
Published in final edited form as: J Chromatogr B Analyt Technol Biomed Life Sci. 2010 Aug 21;878(28):2775–2781. doi: 10.1016/j.jchromb.2010.08.021

Table 2.

Binding parameters obtained for acetohexamide with glycated HSA by frontal analysis and using a two-site modela

High affinity sites Low affinity sites
Type of column Ka1 (× 105 M−1) mL1 (× 10−8 mol) Specific activity (mol/mol HSA) Ka2 (× 103 M−1) mL2 (× 10−8 mol) Specific activity (mol/mol HSA)
HSAb 1.3 (± 0.2) 2.4 (± 0.1) 1.3 (± 0.1) 0.35 (± 0.03) 9.3 (± 5.5) 5.2 (± 3.1)
gHSA1 1.2 (± 0.2) 1.7 (± 0.1) 1.3 (± 0.2) 1.4 (± 0.8) 1.7 (± 0.4) 1.3 (± 0.3)
gHSA2 2.0 (± 0.6) 1.8 (± 0.3) 0.80 (± 0.20) 11 (± 3) 2.4 (± 0.3) 1.1 (± 0.2)
gHSA3 2.0 (± 0.3) 1.5 (± 0.1) 0.80 (± 0.09) 4.1 (± 0.7) 3.0 (± 0.1) 1.6 (± 0.5)
a

The values in parenthesis represent ± 1 S.D. These values were determined by using error propagation and the standard deviations of the slopes and intercepts that were obtained from best-fit lines generated according to Eqn. (3).

b

The results for normal HSA were obtained from Ref. [18] and were acquired using immobilization and chromatographic conditions identical to those used in this current study for glycated HSA.