Akita Keiichi, Fujimura Yukihiro, Bajotto Gustavo, Shimomura Yoshiharu
Department of Materials Science and Engineering, Nagoya Institute of Technology, Nagoya, Japan.
Biosci Biotechnol Biochem. 2009 May;73(5):1189-91. doi: 10.1271/bbb.80749. Epub 2009 May 7.
Inhibition of branched-chain alpha-ketoacid dehydrogenase kinase (BDK) by thiamine pyrophosphate (TPP) was analyzed at two potassium ion (K(+)) concentrations. IC(50) values of 4.6 and 8.0 microM and inhibition constant values of 3.2 and 16.4 microM were obtained in the presence of 20 and 100 mM K(+), respectively. These results suggest that BDK is less sensitive to TPP inhibition under physiological TPP and K(+) concentrations.
在两个钾离子(K⁺)浓度下分析了焦磷酸硫胺素(TPP)对支链α-酮酸脱氢酶激酶(BDK)的抑制作用。在分别存在20 mM和100 mM K⁺的情况下,获得的半数抑制浓度(IC₅₀)值分别为4.6和8.0微摩尔,抑制常数分别为3.2和16.4微摩尔。这些结果表明,在生理TPP和K⁺浓度下,BDK对TPP抑制的敏感性较低。