Determination of binding constants between the antibiotic ristocetin A and D-Ala-D-Ala terminus peptides by affinity capillary electrophoresis

被引:18
作者
Azad, M [1 ]
Hernandez, L [1 ]
Plazas, A [1 ]
Rudolph, M [1 ]
Gomez, FA [1 ]
机构
[1] Calif State Univ Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90032 USA
基金
美国国家科学基金会;
关键词
affinity capillary electrophoresis; antibiotics; binding constants; ristocetin;
D O I
10.1007/BF02492405
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Binding constants between the antibiotic ristocetin A (Rist A) and D-Ala-D-Ala terminus peptides were determined using affinity capillary electrophoresis (ACE). in these experiments two techniques are used to obtain binding constants. In the first, a plug of Rist A and non-interacting standards are injected and electrophoresed. Analysis of the change in the relative migration time ratio (RMTR) of Rist, relative to the non-interacting standards, as a function of the concentration of peptide, yields a value for the binding constant (K-b). in the second, samples of peptide and standards ore injected and electrophoresed in increasing concentrations of Rist A in the running buffer. Analysis using the RMTR yields a K-b. The findings described here demonstrate the advantage of using ACE for estimating binding parameters between antibiotics and ligands.
引用
收藏
页码:339 / 343
页数:5
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