S. Bizzozero

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Peptide substrates of the general structure Ac-Tyr-Ly1-Ly2-..-Lym-NH2 and Ac-Phe-Ly1-NH2 have been synthesized and subjected to alpha-chymotrypsin-catalyzed hydrolysis to collect information on the interactions between the enzyme active site and the amino-acid residues Ly1, Ly2, etc., C-terminal to the susceptible bond of the peptide. For this purpose(More)
A number of peptide-ester substrates of the general structure Ac-Lxn-...-Lx2-Lx1-OMe have been synthesized and their alpha-chymotrypsin-catalyzed hydrolysis studied. The kinetic analysis involved varying the concentration of substrate and methanol product, and measuring rates along the entire progression curve. For the dipeptide esters Ac-Lx2-Lx1-OMe and(More)
Hydrolyses catalyzed by bovine pancreatic trypsin and porcine pancreatic kallikrein were studied using synthetic peptide substrates of the type E chi-L chi 2-L chi 1 decreases Y and E chi-L chi 3-L chi 2-L chi 1 decreases Y with L chi 1 = Arg defining the hydrolysis position (indicated by the arrow). The leaving moiety Y was -OCH3, -NH-C6H4-p-NO2 and(More)
The aim of this paper is to present the results of a research in the design and development of a &#8220;<italic>network user interface</italic>&#8221; application which provides capabilities to locally organise information resulting from searches conducted on a collection of data distributed across a wide area network. A strong requirement which had to be(More)
The kinetics of peptide-bond formation catalyzed by delta-chymotrypsin has been studied for a number of peptide products of different length using fixed concentrations of the acyl component (Ac-Phe-OMe, Ac-Ala-Ala-Phe-OMe, or Ac-Ala-Ala-Tyr-OMe) and varying concentration of the amino component (H-Ala-NH2 or H-Ala-Ala-NH2). The time course of the reactions(More)
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