Amino acids and peptides. LII. Intramolecular aminolysis of amide bonds in derivatives of α,γ-diaminobutyric acid, α,β-diaminopropionic acid, and ornithine

1965 ◽  
Vol 30 (7) ◽  
pp. 2410-2433 ◽  
Author(s):  
K. Poduška ◽  
G. S. Katrukha ◽  
A. B. Silaev ◽  
J. Rudinger
1981 ◽  
Vol 34 (4) ◽  
pp. 395 ◽  
Author(s):  
Leo A Holt ◽  
Brian Milligan

Experiments with the N-benzyloxycarbonyl derivatives of asparagine and glutamine as models show that, in unbuffered solutions, I,I-diacetoxyiodobenzene (1) is more effective than the corresponding trifluoroacetoxy derivative (2) for converting the amide side-chains of proteins to amines. Maximum modification of the glutamine residues of insulin and lysozyme occurs within 1-2 h of treatment with 1 in aqueous methyl cyanide at 20�C, but asparagine residues react more slowly. The amide side-chains are converted to the corresponding amines in at least 90 % yield, as shown by analysis of acid hydrolysates for aspartic acid, lX,p-diaminopropionic acid, glutamic acid and lX,y-diaminobutyric acid. Numerous side-reactions also occur, tyrosine, cystine, methionine, arginine, lysine and N-terminal residues all being modified to some extent.


1998 ◽  
Vol 5 (4) ◽  
pp. 259-262 ◽  
Author(s):  
Chrysostomos Pachatouridis ◽  
Elias A. Couladouros ◽  
Vassilios P. Papageorgiou ◽  
Maria Liakopoulou-Kyriakides
Keyword(s):  

Author(s):  
A. A. Ioganson ◽  
Yu. G. Kovalev ◽  
L. L. Milovanova
Keyword(s):  

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