Successful Application of the Lipase as a Catalyst in the Combinative Approach, Using an Efficient and Selective Iterative Procedure for the Chemo-Enzymatic Alpha-Amino Group Protection in the Natural Amino Acids, Representing the Ornithyl Model System as a Starting Research Pattern: Homogeneous and Heterogeneous Synthesis

Author(s):  
Bayryamov SG
1982 ◽  
Vol 47 (1) ◽  
pp. 210-216 ◽  
Author(s):  
Milan Strašák ◽  
František Bachratý ◽  
Jaroslav Majer

The synthesis and physico-chemical parameters are described of a new complexone based on natural amino acids, viz. ethylenediamine-N,N'-di-S-α-isovalerate (SS-EDDIV). 1H- and 13C-NMR data revealed that the methyl group in the substance are not equivalent. The isomers of the cobalt(III) complex with the asymmetric tetradentate SS-EDDIV ligand were prepared and separated; their characteristics are given. The absolute configuration of two of the five theoretically feasible isomers was determined based on their electronic absorption spectra and circular dichroism data.


Genetics ◽  
1998 ◽  
Vol 150 (3) ◽  
pp. 977-986 ◽  
Author(s):  
Yangsuk Park ◽  
John Hanish ◽  
Arthur J Lustig

Abstract Previous studies from our laboratory have demonstrated that tethering of Sir3p at the subtelomeric/telomeric junction restores silencing in strains containing Rap1-17p, a mutant protein unable to recruit Sir3p. This tethered silencing assay serves as a model system for the early events that follow recruitment of silencing factors, a process we term initiation. A series of LexA fusion proteins in-frame with various Sir3p fragments were constructed and tested for their ability to support tethered silencing. Interestingly, a region comprising only the C-terminal 144 amino acids, termed the C-terminal domain (CTD), is both necessary and sufficient for restoration of silencing. Curiously, the LexA-Sir3N205 mutant protein overcomes the requirement for the CTD, possibly by unmasking a cryptic initiation site. A second domain spanning amino acids 481-835, termed the nonessential for initiation domain (NID), is dispensable for the Sir3p function in initiation, but is required for the recruitment of the Sir4p C terminus. In addition, in the absence of the N-terminal 481 amino acids, the NID negatively influences CTD activity. This suggests the presence of a third region, consisting of the N-terminal half (1-481) of Sir3p, termed the positive regulatory domain (PRD), which is required to initiate silencing in the presence of the NID. These data suggest that the CTD “active” site is under both positive and negative control mediated by multiple Sir3p domains.


Langmuir ◽  
2009 ◽  
Vol 25 (19) ◽  
pp. 11760-11767 ◽  
Author(s):  
Yanning Li ◽  
Brian G. Cousins ◽  
Rein V. Ulijn ◽  
Ian A. Kinloch

2008 ◽  
Vol 19 (3) ◽  
pp. 252-255 ◽  
Author(s):  
Ivan T. Devedjiev ◽  
Stanislav G. Bairyamov ◽  
Vladimira S. Videva

1995 ◽  
Vol 29 (7) ◽  
pp. 454-458 ◽  
Author(s):  
S. A. Kazaryan ◽  
K. P. Grigoryan ◽  
S. N. Airapetyan ◽  
O. L. Mndzhoyan

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