@article{oai:niigata-u.repo.nii.ac.jp:00001509,
 author = {Takehara, Ko and Morinaga, Yuki and Nakashima, Shinya and Matsuoka, Shiro},
 issue = {12},
 journal = {Analytical sciences},
 month = {Dec},
 note = {With the fluorescence probe of 8-anilino-1-naphthalenesulfonate (ANS), the binding modes of terminally substituted alkane analogues (CnX; X = COOH, OH, CHO, NH3, CONH2) to bovine serum albumin (BSA) were investigated using a competitive binding technique. The Scatchard plot of the fluorometric titration of BSA with ANS showed that the maximum binding number of ANS, nmax, was 3.81, with the binding constant, Kbnd, of 1.42 × 106 mol-1 dm3. The binding modes of CnX to BSA were analyzed based on the fluorometric titration of the ANS and BSA mixture with CnX. CnCOOH completely displaced the ANS bound to BSA, whereas CnOH and CnCHO displaced only about 40% of the ANS bound to BSA. In contrast, CnNH2 and CnCONH2 displaced very little bound ANS. By comparing these results, we classified the binding modes of CnX to BSA into three types. Two of them are detectable with the ANS fluorescence and the remaining one is not detectable with the fluorescence.},
 pages = {1571--1575},
 title = {Classification of the Binding Modes in Bovine Serum Albumin Using Terminally Substituted Alkane Analogues},
 volume = {22},
 year = {2006}
}