Interplay between secondary structure and ion binding upon thermoreversible gelation of κ-carrageenan

2020 ◽  
Vol 227 ◽  
pp. 115342 ◽  
Author(s):  
O.N. Makshakova ◽  
D.A. Faizullin ◽  
Yu.F. Zuev
1999 ◽  
Vol 17 (3) ◽  
pp. 473-480 ◽  
Author(s):  
M. Purcell ◽  
A. Novetta-Delen ◽  
H. Arakawa ◽  
H. Malonga ◽  
H. A. Tajmir-Riahi

2019 ◽  
Vol 150 (17) ◽  
pp. 174904
Author(s):  
Fumihiko Tanaka ◽  
Yoshiyuki Nakagawa ◽  
Seiichi Ohta ◽  
Taichi Ito

Author(s):  
John P. Robinson ◽  
J. David Puett

Much work has been reported on the chemical, physical and morphological properties of urinary Tamm-Horsfall glycoprotein (THG). Although it was once reported that cystic fibrotic (CF) individuals had a defective THG, more recent data indicate that THG and CF-THG are similar if not identical.No studies on the conformational aspects have been reported on this glycoprotein using circular dichroism (CD). We examined the secondary structure of THG and derivatives under various conditions and have correlated these results with quaternary structure using electron microscopy.THG was prepared from normal adult males and CF-THG from a 16-year old CF female by the method of Tamm and Horsfall. CF female by the method of Tamm and Horsfall.


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