Sclavo Spa

Eniricerche S.p.a.

Giuseppe C Viscomi

Franco Cardinali

Maria G Longobardi

Paolo Rappuoli

Alessandra Ziggiotti

A process is described for the purification of recombinant human beta interferon which comprises the use of three chromatographic stages carried out in series, utilizing as stationary phases: glass particles of controlled porosity, cation exchange polymer resins and polymer resins able to complex heavy metals.

Process for the purification of recombinant human beta interferon, beta

This invention firstly provides a method for purifying particular compounds of peptide or pseudo-peptide structure in which the number of protonable basic functions is greater than the number of acid functions and which have a molecular weight of less than 1000 daltons, by ion exchange displacement chromatography. In the method of the present invention the stationary phase used is a cationic exchange resin or a cross-linked polymer matrix activated with acid groups; the transporter solvent used is water if the compound to be purified already possesses at least one net positive charge, or aqueous dilute solutions of inorganic or strong organic acids which protonate the basic groups of the peptide or pseudo-peptide to be separated without modifying the structure of the peptide compound, such as acetic acid, trifluoroacetic acid, formic acid, hydrochloric acid or sulphuric acid; the displacer compound used is a triethylenetetraammonium salt.

Method for purifying low molecular weight compounds of peptide or

A new mono-silylating agent of general formula (I)

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Siena, Italy

Giuseppe C Viscomi