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  • 1
    ISSN: 1434-601X
    Keywords: 21.10.Dr ; 23.90.+w ; 27.40.+z
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Neutron-deficient isotopes with Z=21 to 26 have been produced as projectile-like fragments of an intense58Ni GANIL beam of 69 MeV/nucleon. The nuclei selected by the upgraded LISE3 spectrometer were identified and implanted in a silicon detector telescope. The43Cr,47Fe and46Fe isotopes were identified for the first time whereas45Fe,45Mn,44Mn and42V were not observed, indicating probable instability of these nuclei against particle emission. Measurements of the half-lives of43Cr and46Mn have been performed and the analysis of their measured beta-delayed proton spectra has given, through the isobaric multiplet mass equation, an empirical estimation of their masses. Half-lives of44Cr,43V,47Fe and46Fe have also been measured. A discussion of various mass predictions for nuclei at the proton drip-line is given.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 3 (1988), S. 130-137 
    ISSN: 0887-3585
    Keywords: peptide synthesis ; chymotrypsin specificity ; polyethylene glycol ; nonaqueous solvents ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Chymotrypsin modified with polyethylene glycol was successfully used for peptide synthesis in organic solvents. The benzene-soluble modified enzyme readily catalyzed both aminolysis of N-benzoyl-L-tyrosine p-nitroanilide and synthesis of N-benzoyl-L-tyrosine butylamide in the presence of trace amounts of water. A quantitative reaction was obtained when either hydrophobic or bulky amides of L- as well as D-amino acids were used as acceptor nucleophiles, while almost no reaction occurred with free amino acids or ester derivativesThe acceptor nucleophile specificity of modified chymotrypsin as a catalyst in the formation of both amide and peptide bonds in organic solvents was quite comparable to that in aqueous solution as well as to that of the leaving group in hydrolysis reactions. By contrast, the substrate specificity of modified chymotrypsin in organic solvents was different from that in water since arginine and lysine esters were found to be as effective as aromatic amino acids to form the acyl-enzyme with subsequent synthesis of a peptide bond.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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