Issue 8, 2001
From the journal:

Chemical Communications

Antibody catalyzed modification of amino acids. Efficient hydrolysis of tyrosine benzoateElectronic supplementary information (ESI) available: the synthesis and characterization of compound 2, preparation of the immunogenic conjugate, preparation and purification of monoclonal antibodies, experimental details for kinetic studies and Lineweaver-Burk plots. See http://www.rsc.org/suppdata/cc/b1/b100450f/

Fabio Benedetti,*a   Federico Berti,*a   Alfonso Colombatti,b   Massimiliano Flego,a   Lucia Gardossi,c   Paolo Lindac  and  Silvia Peressinia  

* Corresponding authors

a Dipartimento di Scienze Chimiche, Università di Trieste, Via Giorgieri 1, Trieste, Italy.
E-mail: berti@dsch.univ.trieste.it;
Fax: + 39 40 6763903

b Dipartimento di Scienze e Tecnologie Biomediche, Università di Udine, and CRO – IRCSS, Aviano, P.le Kolbe 4, Udine, Italy

c Dipartimento di Scienze Farmaceutiche, Università di Trieste, P.le Europa 1, Trieste, Italy

Abstract

Esterase antibody 522c2, the first example of a catalytic antibody specifically programmed to control the reactivity of functional groups on the side chain of tyrosine, accelerates the hydrolysis of benzoate esters of L-tyrosine and tyrosine-containing dipeptides by a factor of 104 and is moderately active against other benzoate esters.

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Supplementary files

Article information

DOI
https://doi.org/10.1039/B100450F
Article type
Communication
Submitted
11 Jan 2001
Accepted
08 Mar 2001
First published
29 Mar 2001

Chem. Commun., 2001, 715-716

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Antibody catalyzed modification of amino acids. Efficient hydrolysis of tyrosine benzoate

F. Benedetti, F. Berti, A. Colombatti, M. Flego, L. Gardossi, P. Linda and S. Peressini, Chem. Commun., 2001, 715 DOI: 10.1039/B100450F

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