Probing Conformational Change of Bovine Serum Albumin–Dextran Conjugates under Controlled Dry Heating

2015 ◽  
Vol 63 (16) ◽  
pp. 4080-4086 ◽  
Author(s):  
Shuqin Xia ◽  
Yunqi Li ◽  
Qin Zhao ◽  
Ji Li ◽  
Qiuyang Xia ◽  
...  
1971 ◽  
Vol 49 (12) ◽  
pp. 1267-1275 ◽  
Author(s):  
D. E. Goldsack ◽  
P. M. Waern

Pressure jump kinetic studies of the conformational change occurring in bovine serum albumin in neutral solutions have been carried out over the pH range 6.5–9.5. Two distinct relaxation effects are observed at each pH. The faster relaxation is attributed to binding of the dye to the protein, and the slower relaxation is related to the conformational change occurring in the protein. This slower relaxation effect is pH dependent with a maximum value near pH 8. Detailed analysis of these data leads to a mechanism for the conformational change which indicates that the one form of the protein has an ionizable group with a pK of 8.7 which changes to a pK of 6.7 when the protein undergoes the conformational change. A simple iterative procedure is given for analyzing the pH dependence of a relaxation time constant for a cyclic mechanism involving only one ionizing group controlling the conformational change.


2017 ◽  
Vol 45 (3) ◽  
pp. 489-494 ◽  
Author(s):  
Takamasa Okumura ◽  
Kazuki Yamada ◽  
Taro Yaegashi ◽  
Katsuyuki Takahashi ◽  
Bunei Syuto ◽  
...  

2014 ◽  
Vol 118 (42) ◽  
pp. 12207-12214 ◽  
Author(s):  
Shulian He ◽  
Mei Huang ◽  
Wei Ye ◽  
Dechao Chen ◽  
Shuai He ◽  
...  

1989 ◽  
Vol 8 (5) ◽  
pp. 653-659 ◽  
Author(s):  
Kunio Takeda ◽  
Akira Wada ◽  
Kazuo Yamamoto ◽  
Yoshiko Moriyama ◽  
Koichiro Aoki

1975 ◽  
Vol 253 (6) ◽  
pp. 506-507
Author(s):  
Haruyuki Kanehiro ◽  
Jiro Komiyama ◽  
Toshiro Iijima

Biochemistry ◽  
1971 ◽  
Vol 10 (17) ◽  
pp. 3217-3221 ◽  
Author(s):  
S. H. De Bruin ◽  
B. J. M. Harmsen ◽  
L. H. M. Janssen ◽  
J. F. Rodrigues de Miranda ◽  
G. A. J. Van Os

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