Kinetics of transfer in aqueous solution of ferriprotoporphyrin IX from human serum albumin to sperm whale apomyoglobin

Biopolymers ◽  
1982 ◽  
Vol 21 (12) ◽  
pp. 2399-2411 ◽  
Author(s):  
G. Blauer ◽  
J. Silfen
1989 ◽  
Vol 54 (2) ◽  
pp. 536-543 ◽  
Author(s):  
Josef Chmelík ◽  
Pavel Anzenbacher ◽  
Vítěz Kalous

The renaturation of the two main components of human serum albumin, i.e. of mercaptalbumin and nonmercaptalbumin, was studied polarographically. It has been demonstrated that renaturation of both proteins after 1-min denaturation in 8M urea is reversible. By contrast, renaturation after 200 min denaturation in 8M urea is an irreversible process; the characteristics of renatured mercaptalbumin differ more from the properties of the native protein than the characteristics of nonmercaptalbumin. The studies of the kinetics of renaturation of both proteins have shown that the renaturation can be represented by a two-state model. This means that the existence of stable intermediary products during the renaturation process was not determined polarographically.


Chirality ◽  
2002 ◽  
Vol 14 (5) ◽  
pp. 442-448 ◽  
Author(s):  
Ilona Fitos ◽  
J�lia Visy ◽  
Julianna Kardos

Langmuir ◽  
2001 ◽  
Vol 17 (17) ◽  
pp. 5189-5195 ◽  
Author(s):  
J. M. Ruso ◽  
D. Attwood ◽  
M. García ◽  
P. Taboada ◽  
L. M. Varela ◽  
...  

2014 ◽  
Vol 201 ◽  
pp. 177-184 ◽  
Author(s):  
Lihua Lu ◽  
Hong-Zhang He ◽  
Hai-Jing Zhong ◽  
Li-Juan Liu ◽  
Daniel Shiu-Hin Chan ◽  
...  

1979 ◽  
Vol 181 (3) ◽  
pp. 779-781 ◽  
Author(s):  
D W Hutchinson ◽  
D S Mutopo

A one-step procedure has been developed for the preparation of [3H]bilirubin IX-alpha in good yield from unlabelled bilirubin. Irradiation of an aqueous solution of [3H]bilirubin IX-alpha in the presence of human serum albumin results in the covalent attachment of the bilirubin to the protein. Preliminary degradation studies have been carried out to locate the site of attachment of the bilirubin to the albumin.


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