scholarly journals The interaction of triethyltin with a component of guinea-pig liver supernatant. Evidence for histidine in the binding sites

1970 ◽  
Vol 120 (1) ◽  
pp. 151-157 ◽  
Author(s):  
M. S. Rose ◽  
E. A. Lock

A protein fraction was isolated from guinea-pig liver that binds triethyltin with an affinity of approx. 2×106m−1 at pH8.0. It was shown that the protein responsible for binding 70% of the triethyltin found in guinea-pig liver after injection of radioactively labelled triethyltin is at most a few per cent of the total liver protein. Evidence is presented from the kinetics of loss of binding and loss of certain amino acids on photo-oxidation with either Methylene Blue or Rose Bengal that each binding site consists of two histidine residues.

1962 ◽  
Vol 40 (1) ◽  
pp. 983-987 ◽  
Author(s):  
Felix Friedberg

Apoferritin isolated from livers of guinea pigs and characterized by a s°w,20 of 17.7 and a pI of 4.8 (in acetate buffer Γ/2 0.1) was hydrolyzed with 5.7 N HCl for 22 and 44 hours and its amino acid composition determined. The protein appears rich in dicarboxylic acids and in leucine. The content of sulphur-containing amino acids is fairly small.


FEBS Letters ◽  
1992 ◽  
Vol 307 (2) ◽  
pp. 177-180 ◽  
Author(s):  
Y. Takeuchi ◽  
P.J. Birckbichler ◽  
M.K. Patterson ◽  
K.N. Lee

1989 ◽  
Vol 180 (1) ◽  
pp. 161-166 ◽  
Author(s):  
Sylvie NURY ◽  
Jean-Claude MEUNIER ◽  
Annette MOURANCHE

1962 ◽  
Vol 40 (8) ◽  
pp. 983-987 ◽  
Author(s):  
Felix Friedberg

Apoferritin isolated from livers of guinea pigs and characterized by a s°w,20 of 17.7 and a pI of 4.8 (in acetate buffer Γ/2 0.1) was hydrolyzed with 5.7 N HCl for 22 and 44 hours and its amino acid composition determined. The protein appears rich in dicarboxylic acids and in leucine. The content of sulphur-containing amino acids is fairly small.


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