Kinetics of binding of methyl .alpha.- and .beta.-D-galactopyranoside to peanut agglutinin: a carbon-13 nuclear magnetic resonance study

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DOIResolve DOI: http://doi.org/10.1021/bi00515a030
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TypeArticle
Journal titleBiochemistry
ISSN0006-2960
1520-4995
Volume20
Issue12
Pages34993504
AbstractThe binding kinetics of methyl α- and methyl β-D-galactopyranoside to the anti-T lectin from peanuts were studied by ¹³C NMR, employing methyl galactopyranosides specifically enriched in ¹³C at C-1. Association and dissociation rate constants, as well as their activation parameters, are reported. The association rate constants, 4.6 X l0⁴ M⁻¹ s⁻¹ for the α-galactopyranoside and 3.6 X l0⁴ M⁻¹ s⁻¹ for the β-galactopyranoside, are several orders of magnitude below those expected for a diffusion-controlled process. For both anomers, the association rate constant was temperature independent, implying that the association process occurs without a significant activation enthalpy. However, a considerable association activation entropy was found for both ligands. The dissociation rate constants were in the range of 9-46 s⁻¹ within a temperature range of 5-35 ºC for the a-galactopyranoside, and in the range of 9-39 s⁻¹ within a temperature range of 5-25 ºC for the β-galactopyranoside. A considerable dissociation activation enthalpy of ca. 10 kcal mol⁻¹ was found for both anomers. A two-step binding model, consistent with the present NMR data and with previous UV and CD spectroscopic data, is presented.
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedYes
NRC numberNEUROHR1981
NPARC number9369771
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Record identifier7c235c97-e1ac-460c-a1ca-9048afb837ee
Record created2009-07-10
Record modified2017-03-24
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