Luedemann, Hans-Dietrich and Bernhardt, Günther and Jaenicke, Rainer and Koenig, Helmut and Stetter, Karl Otto (1984) Biomolecules are unstable under "black smoker" conditions. Naturwissenschaften 71 (11), pp. 583-586.
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The effects of high hydrostatic pressure on hydrolysis and hydrothermal degrdn. of amino acids, polyglycine, and thermophilic bacteria were studied. Most amino acids, after 6 h incubation on 250 Deg and 260 bar, pH 2 and 7.6, were transformed or decompd. Glycine, alanine, and NH3 increased drastically, suggesting that they are degrdn. products. To det. the stability of the peptide bond, ...
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|Additional Information (public):||CAN 102:41866 6-7 General Biochemistry 25718-94-9; 25734-27-4 Role: RCT (Reactant), RACT (Reactant or reagent) (degrdn. and hydrolysis of, at high temp. and pressure, thermophilic microorganism in relation to)|
|Institutions:||Chemistry and Pharmacy > Institute of Pharmacy > Pharmaceutical/Medicinal Chemistry II (Prof. Buschauer)|
|Keywords:||Amino acids Role: RCT (Reactant), RACT (Reactant or reagent) (degrdn. and hydrolysis of, at high temp. and pressure, thermophilic microorganism in relation to); Pyrodictium occultum (high temp. and pressure effect on amino acids of, viability in relation to); Heat (on biol. mols. and microorganisms); Bacteria (thermophilic, high temp. and pressure effect on amino acids of, viability in relation to); heat thermophilic bacteria degrdn amino acid degrdn heat pressure peptide degrdn heat pressure|
|Dewey Decimal Classification:||500 Science > 570 Life sciences|
|Refereed:||Yes, this version has been refereed|
|Created at the University of Regensburg:||Yes|
|Deposited on:||15 Jan 2009 15:18|
|Last modified:||05 Aug 2009 13:50|