Celltech Limited

Peter Anthony Lowe

Stephen Keith Rhind

Norman H Carey

Michael T Doel

Sarojani Angal

Christopher C Hentschel

Joyce A Schoemaker

Alan D Bennett

Fiona A Marston

Timothy J Harris

A human gastric lipase protein for use in the treatment of lipase deficiency. A process is described for producing gastric lipase using recombinant DNA technology to produce a host organism (for example E. coli) capable of producing a methionine-gastric lipase or precursor of the gastric lipase which may be cleaved to yield the gastric lipase. The host organism is transformed with a vector including a gene coding for a methionine-gastric lipase or a precursor of gastric lipase. The precursor protein is for example, pregastric lipase protein, or a fusion protein comprising gastric lipase and a heterologous protein. A pharmaceutical composition in unit dosage or liquid form is described.

Lipase from human gastric mucosal tissue

DNA encoding lipase from human gastric mucosal tissue

In a process for the production of a soluble native protein, such as immunoglobulin or methionine-prochymosin, in which an insoluble form of the protein is produced by a host organism transformed with a vector including a gene coding for the protein, the insoluble form of the protein is reversibly denatured in an alkaline aqueous solution at a pH selected to promote dissociation of a group or groups of the protein involved in maintaining the conformation of the protein, and the protein is subsequently allowed to renature by reducing the pH of the solution below a pH effective to denature the protein to produce the soluble native form of the protein. The pH of the alkaline aqueous is suitably in the range 9.0 to 11.5.

Process for the recovery of recombinantly produced protein from

The production of recombinant chymosin is disclosed in which an insoluble form of chymosin precursor is produced by a bacterial host cell transformed by a vector including a coding sequence for said precursor. Solubilization of said insoluble form of chymosin precursor is accomplished using urea at a concentration of at least 7M or guanidine hydrochloride at a concentration of at least 6M prior to cleaving said precursor to form chymosin. Said solubilization preferably additionally involves the denaturation of said precursor in an alkaline aqueous solution, e.g., at a pH between a 9 and 11.5

Process for the recovery of recombinantly produced chymosin from

A process for the production of a fusion protein comprising an active portion of a chloramphenicol acetyltransferase (CAT) protein and a polypeptide. The fusion protein may be purified using CAT substrate affinity chromatography. The eucaryotic polypeptide may be calcitonin or a dervative thereof such as calcitonin-glycine. Other polypeptides described include enzymes such as chymosin, prochymosin and preprochymosin, hormones such as ACTH, insulins, and growth hormones and antigenic polypetides such as foot and mouth disease virus antigenic polypetide. The fusion protein may be cleaved at a site susceptible to selective enzymic or chemical cleavage to produce free polypeptide. The fusion protein may be used as an immunogen.

C-terminal CAT fusion protein and process of preparation by recombinant

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Reading, United Kingdom

Peter Anthony Lowe