Equilibrium dialysis and cell binding studies on Bandeiraea simplicifolia lectin.
نویسندگان
چکیده
Equilibrium dialysis studies on the binding of the blood group B-specific Bandeiraea simplicifolia lectin to methyl alpha-D-galactopyranoside demonstrated the existence of one carbohydrate binding site per subunit for the tetrameric protein, with an intrinsic association constant of 8.6 x 10(4) (M) (-1) at 2 degrees and 3.3 x 10(4) (M)(-1) at 20 degrees. These values correspond to a free energy of binding, ΔG(0') (pH 7.2), of -6.21 kcal/mol and-6.06 kcal/mol at 2 degrees and 20 degrees, respectively. The sites appeared homogeneous and noninteracting. B. simplicifolia lectin receptor sites per human B erythrocyte varied from 0.72 x 10(5) to 1.34 x 10(5) with an apparent association constant of 1.1 x 10(7) (M)(-1) to 2.9 x 10(7) (M)(-l). The binding characteristics of B. simplicifolia lectin are compared to other purified lectins.
منابع مشابه
An immunochemical study of the combining sites of the second lectin isolated from Bandeiraea simplicifolia (BS II).
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 250 17 شماره
صفحات -
تاریخ انتشار 1975