Hoffmann-la Roche Inc.

F. Hoffmann-la Roche Ag

Klaus Reichert

Josef Burg

Hartmut Ernst Schurig

Axel Schroth

Axel Wessner

Christoph Seidel

Thomas Meier

Rainer Schmuck

Wilhelm Tischer

Eva Hoess

Bernd Schneidinger

Gabriele Pestlin

Friedrich Popp

Tatjana Buerker

Christian Haase

Hartmut Schurig

A method and an apparatus () for electrostatically discharging a primary packaging container () made of plastics are disclosed. The method comprises moving a primary packaging container () to be electrostatically discharged so as to pass at least one electrode (), applying an alternating voltage to the electrode () so as to generate ionized air in a vicinity of the electrode (), and rotating the primary packaging container () in the vicinity of the electrode () so as to be contacted by the ionized air. The apparatus () comprises at least one electrode () adapted to generate ionized air in a vicinity of the electrode () and a moving path () for moving a primary packaging container () to be electrostatically discharged, wherein the moving path () is formed such that the primary packaging container () is adapted to pass the electrode () and to be rotated in the vicinity of the electrode () so as to be contacted by the ionized air.

Method and apparatus for electrostatically discharging a primary packaging container made of plastics

The invention is a method for the purification of mono-PEGylated erythropoietin using two cation exchange chromatography steps wherein the same type of cation exchange material is used in both cation exchange chromatography steps and a method for producing a mono-PEGylated erythropoietin in substantially homogeneous form.

Purification of pegylated polypeptides

The current invention comprises a method for the regeneration of a cation exchange chromatography column.

Chromatographic methods

A process is disclosed for the production of an antifusogenic peptide by producing a fusion peptide of a length of about 14 to 70 amino acids in a prokaryotic host cell, comprising the steps, under such conditions that inclusion bodies of said fusion peptide are formed, of: (a) expressing in said host cell a nucleic acid encoding said fusion peptide consisting of a first peptide which is an antifusogenic peptide of a length of about 10 to 50 amino acids and a second peptide of a length of about 4 to 30 amino acids, said first peptide being N-terminally linked to said second peptide; (b) cultivating said host cell to produce said inclusion bodies; and (c) recovering said antifusogenic peptide from said inclusion bodies, wherein said recovered antifusogenic peptide consists of said fusion peptide or a peptide comprising the antifusogenic peptide of about 10 to 50 amino acids and which is a fragment cleaved from said fusion peptide. Inclusion bodies of the peptides are disclosed. Also disclosed is a nucleic acid encoding the fusion peptide consisting of a first peptide which is an antifusogenic peptide selected from the group of SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, and said sequences further consisting of glycine at the C terminal end, N-terminally linked to the second peptide.

Nucleic acids encoding fusion peptides

A process is provided for producing an antifusogenic peptide by producing a fusion peptide of from about 14 amino acids up to 70 amino acids in a prokaryotic host cell under conditions in which inclusion bodies are formed. The antifusogenic peptide recovered from the inclusion bodies is a fragment cleaved from the fusion peptide which comprises an antifusogenic peptide.

Process for making antifusogenic fusion peptides that form inclusion bodies

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Oberhausen, Germany

Klaus Reichert