Pii: 0003-2697(89)90213-3
نویسندگان
چکیده
A new titration calorimeter is described and results are presented for the binding of cytidine 2’-monophosphate (2’CMP) to the active site of ribonuclease A. The instrument characteristics include very high sensitivity, rapid calorimetric response, and fast thermal equilibration. Convenient software is available for instrument operation, data collection, data reduction, and deconvolution to obtain least-squares estimates of binding parameters n, AH”, AS’, and the binding constant K. Sample through-put for the instrument is high, and under favorable conditions binding constants as large as 10’ M-’ can be measured. The bovine ribonuclease A (RNase)/S’CMP system was studied over a 50-fold range of RNase concentration and at two different temperatures. The binding constants were in the lo6 to lo6 M-’ range, depending on conditions, and heats of binding ca. -16,000 cal/mol. Repeat determinations suggested errors of only a few percent in n, AH”, and K values over the most favorable concentration range.
منابع مشابه
Introducing color into stacking gels makes sample loading easy.
0003-2697/$ see front matter 2007 Elsevier Inc. All rights reserved. doi:10.1016/j.ab.2007.04.002 * Corresponding author. E-mail address: [email protected] (Y. Ryabov). Fig. 1. Traditional (left half of the figure) and new (right half of the figure) rend gels before loading; bottom panels show the scans of the processed gels. I 4%-acrylamide stacking buffer (upper right). The performance of th...
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