A. Könnecke

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The kinetic parameters Km and kcat and the proteolytic coefficients kcat/Km for the hydrolysis of eighteen Z(benzyloxycarbonyl)-dipeptide methyl esters with variation of the residues in P1 and P2 position catalyzed by thermitase at pH 8 and 55 degrees C are reported. The results indicate that an integral part of both subsites, S1 and S2, are hydrophobic(More)
One major problem in protease-catalyzed peptide synthesis is the occurrence of unwanted proteolytic side reactions. The objective of this study was to demonstrate that specific acyl donor esters can efficiently prevent the enzymatic hydrolysis of the peptide product. As a model system, we have studied the alpha-chymotrypsin-catalyzed synthesis of peptides(More)
The affinity of N-acyl-L-phenylalanine 4-nitroanilides for chymotrypsin is enhanced as the hydrophobicity of non-amino acid residues in the P2-position of the substrates increases, whereas kcat remains nearly constant. On the other hand, if alanine or leucine is in the P2-position kcat increases with decreasing KM.
Carbohydrate-derived polymers are activated by the chloroformate N-chlorocarbonyloxy-5-norbornene-2.3-dicarboximide (ClCOONB). The advantages of this activation method are presented. The application of bead cellulose as adsorbent for biomedical and biotechnological purposes is demonstrated. Examples for immunoglobulin purification, streptavidin isolation,(More)
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