%0 Journal Article
%T Studies on the Binding Mechanism of  VB<sub>1</sub> and VB<sub>9</sub> with Trypsin
%A Yan Gao
%A Congying Shao
%A Wanru Ji
%A Min Xiao
%A Fan Yi
%A Tong Zhou
%A Yanqin Zi
%J American Journal of Analytical Chemistry
%P 771-775
%@ 2156-8278
%D 2013
%I Scientific Research Publishing
%R 10.4236/ajac.2013.412094
%X <p class=\"MsoNormal\" style=\"text-align:justify;\">
	<span lang=\"EN-US\"><span style=\"font-family:Verdana;\">The binding characteristics of vitamin B</span><sub><span style=\"font-family:Verdana;\">1</span></sub><span style=\"font-family:Verdana;\"> (VB</span><sub><span style=\"font-family:Verdana;\">1</span></sub><span style=\"font-family:Verdana;\">)
and vitamin B</span><sub><span style=\"font-family:Verdana;\">9</span></sub><span style=\"font-family:Verdana;\"> (VB</span><sub><span style=\"font-family:Verdana;\">9</span></sub><span style=\"font-family:Verdana;\">) with </span><span style=\"font-family:Verdana;\">trypsin were investigated by fluorescence spectrometry and UV/vis spectrophotometry
under simulated physiological conditions. With the addition of VB</span><sub><span style=\"font-family:Verdana;\">1</span></sub><span style=\"font-family:Verdana;\"> or VB</span><sub><span style=\"font-family:Verdana;\">9</span></sub><span style=\"font-family:Verdana;\">, the intrinsic fluorescence emission intensity of trypsin was
quenched by the nonradiative energy transfer mechanism. The fluorescence
quenching process of trypsin may be mainly governed by a static quenching
mechanism. The binding parameters such as the binding constants and the number
of binding sites can be evaluated by fluorescence quenching experiments. The
numbers of the apparent binding constant </span><i><span style=\"font-family:Verdana;\">K</span><sub><span style=\"font-family:Verdana;\">b</span></sub></i><span style=\"font-family:Verdana;\"> of VB</span><sub><span style=\"font-family:Verdana;\">1</span></sub><span style=\"font-family:Verdana;\">-trypsin at different temperatures were 0.4948 and 4.8340 กม</span></span><span lang=\"EN-US\"> </span><span lang=\"EN-US\"><span style=\"font-family:Verdana;\">10</span><sup><span style=\"font-family:Verdana;\">4</span></sup><span style=\"font-family:Verdana;\"> L/mol and the numbers of binding sites </span><i><span style=\"font-family:Verdana;\">n</span></i><span style=\"font-family:Verdana;\"> were 0.9359 and 1.1820. Similarly, the numbers of the apparent binding constant </span><i><span style=\"font-family:Verdana;\">K</span><sub><span style=\"font-family:Verdana;\">b</span></sub></i><span style=\"font-family:Verdana;\"> of VB</span><sub><span style=\"font-family:Verdana;\">9</span></sub><span style=\"font-family:Verdana;\">-trypsin
at different temperatures were 5.9310 and 13.040 กม</span></span><span lang=\"EN-US\"> </span><span lang=\"EN-US\"><span style=\"font-family:Verdana;\">10</span><sup><span
%K Trypsin
%K VB&lt
%K sub&gt
%K 1&lt
%K /sub&gt
%K and VB&lt
%K sub&gt
%K 9&lt
%K /sub&gt
%K Fluorescence Spectrometry
%K Nonradiative Energy Transfer Mechanism
%U http://www.scirp.org/journal/PaperInformation.aspx?PaperID=41337