Unfolding pathway of myoglobin: effect of denaturants on solvent accessibility to tyrosyl residues detected by second-derivative spectroscopy

Biochemistry ◽  
1987 ◽  
Vol 26 (8) ◽  
pp. 2130-2134 ◽  
Author(s):  
Raffaele Ragone ◽  
Giovanni Colonna ◽  
Ettore Bismuto ◽  
Gaetano Irace
1985 ◽  
Vol 31 (2) ◽  
pp. 279-281 ◽  
Author(s):  
J Parks ◽  
H G Worth

Abstract In this procedure hemoglobin is converted to its reduced form and the magnitude of the zero-order spectral shift of the reduced hemoglobin peak at 430 nm to the carboxyhemoglobin peak at 418 nm is determined by second-derivative spectrum analysis. The method is simple, straightforward to set up, and rapid. A result may be obtained within 15 min of receiving the sample. It is sufficiently sensitive to differentiate carboxyhemoglobin concentration in the blood of smokers and nonsmokers.


1992 ◽  
Vol 16 (4) ◽  
pp. 214-216 ◽  
Author(s):  
Chiaki Fuke ◽  
Kiyoshi Ameno ◽  
Setsuko Ameno ◽  
Takahiro Kirlu ◽  
Toyohiko Shinohara ◽  
...  

1999 ◽  
Vol 23 (7) ◽  
pp. 586-590 ◽  
Author(s):  
Michel Imbenotte ◽  
Nathalie Azaroual ◽  
Daniel Mathieu ◽  
Bernard Cartigny ◽  
Gaston Vermeersch ◽  
...  

1982 ◽  
Vol 123 (1-2) ◽  
pp. 121-126 ◽  
Author(s):  
Alain Bertrand ◽  
Claude Cox ◽  
Pierre Foucart ◽  
Jean Buret

Biochemistry ◽  
1984 ◽  
Vol 23 (8) ◽  
pp. 1871-1875 ◽  
Author(s):  
Raffaele Ragone ◽  
Giovanni Colonna ◽  
Ciro Balestrieri ◽  
Luigi Servillo ◽  
Gaetano Irace

1992 ◽  
Vol 37 (4) ◽  
pp. 907-913 ◽  
Author(s):  
William G. Crumpton ◽  
Thomas M. Isenhart ◽  
Paul D. Mitchell

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