Action of surface-active substances on biological membranes V. Hemolytic, lytic and membrane-perturbing effects of N-lauroyl derivatives of amino acids with aliphatic side chains

1979 ◽  
Vol 257 (9) ◽  
pp. 953-958 ◽  
Author(s):  
B. Zaslavsky ◽  
N. Ossipov ◽  
A. Y. Lisichkin ◽  
Y. A. Davidovich ◽  
S. Rogozhin
1973 ◽  
Vol 51 (12) ◽  
pp. 1915-1919 ◽  
Author(s):  
John R. McDermott ◽  
N. Leo Benoiton

Reaction of N-benzyloxycarbonyl derivatives of aliphatic amino acids, and threonine, aspartic, and glutamic acids whose side-chains were protected with the t-butyl group, gave the corresponding N-methylamino acid derivatives in good yields. The methionine derivative could be obtained by using only one mol of methyl iodide. Derivatives of threonine, and aspartic and glutamic acids whose side-chains were not protected could not be methylated. Analysis of the crude products of methylation in three cases showed that they contained 0–1% of racemized material.


1979 ◽  
Vol 556 (2) ◽  
pp. 314-321 ◽  
Author(s):  
Boris Yu. Zaslavsky ◽  
Nicolai N. Ossipov ◽  
Sergei V. Rogozhin ◽  
Yurii L. Sebyakin ◽  
Ludmila V. Volkova ◽  
...  

1978 ◽  
Vol 507 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Boris Yu. Zaslavsky ◽  
Nicolai N. Ossipov ◽  
Vladimir S. Krivich ◽  
Lidia P. Baholdina ◽  
Sergei V. Rogozhin

1996 ◽  
Vol 49 (5) ◽  
pp. 541 ◽  
Author(s):  
BM Duggan ◽  
RL Laslett ◽  
JFK Wilshire

An investigation has been carried out into the Schlack-Kumpf reaction, i.e., the reaction of amino acids with a mixture of acetic anhydride, acetic acid and sodium thiocyanate (occasionally ammonium thiocyanate was used). Particular emphasis was placed on the reactions with amino acids containing sensitive or functional side chains, i.e., serine, threonine , arginine , proline , lysine, histidine , cysteine , and aspartic and glutamic acids. The reaction of serine, and of certain of its O- and N-substituted derivatives, takes an unusual course to give an acetylated thiohydantoin derivative of cysteine. Correspondingly, threonine gives an acetylated thiohydantoin derivative of β- methylcysteine. Similar reactions occurred with the 3-phenylthiohydantoin derivatives of serine and of threonine to give acetylated thiohydantoin derivatives of cysteine and of β-methylcysteine respectively.


1996 ◽  
Vol 49 (5) ◽  
pp. 551 ◽  
Author(s):  
F Casagranda ◽  
BM Duggan ◽  
A Kirkpatrick ◽  
RL Laslett ◽  
JFK Wilshire

An investigation has been carried out into the thiocyanate degradation (AcOH/Ac2O/HSCN) procedure as it relates to the C-terminal sequencing of peptides, particular emphasis being placed on the sequencing of amino acid residues containing sensitive or functional side chains. Attempted C-terminal sequencing of several serine- and threonine -containing peptides stopped at these particular residues, and did not proceed further. It is concluded that sequencing of most of the common amino acids is achievable but that significant problems will have to be overcome before routine sequencing of proline , serine, threonine, arginine , and, in particular, aspartic and glutamic acids can be claimed. The action of base on the thiohydantoin derivatives of N,S- diacetylcysteine and N,S- diacetyl-β-methylcysteine causes β-elimination of thioacetic S-acid to give the corresponding olefinic thiohydantoins.


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