Process for the preparation of active somatotropin from...

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Hormones – e.g. – prolactin – thymosin – growth factors – etc.

Reexamination Certificate

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C530S311000, C530S324000, C530S344000, C530S824000, C530S825000, C530S397000

Reexamination Certificate

active

06987173

ABSTRACT:
A process for the preparation of biologically active somatotropin from inclusion bodies of a recombinant host cell containing an inactive form of said somatotropin protein comprises the steps of:(a) contacting the inclusion bodies with an aqueous alcohol solution at an alkaline pH to solubilize said protein; and(b) bringing the solubilized protein into contact with a mild oxidizing agent to refold and form intramolecular disulfide bonds between cysteine residues of said protein.

REFERENCES:
patent: 5109117 (1992-04-01), Ho
Brems, et al., “The Kinetics of Bovine Growth Hormone Folding are Consistent With a Framework Model” The Journal of Biological Chemistry, vol. 262, No. 6: 1987 pp. 2590-2596.
Brems, et al., “Equilibrium Denaturation of Pituitary-and Recombiant-Derived Bovine Growth Hormone” Biochemistry, vol. 24, No. 26; 1985, pp. 7662-7668.
Brems, et al., “Characterization of an Associated Equilibrium Folding Intermediate of Bovine Growth Hormone” Biochemistry, vol. 25, No. 21; 1986, pp. 6539-6543.
Brems, et al., “Helical Formation in Isolated Fragments of Bovine Growth Hormone” Biochemistry, vol. 26, No. 24; 1987, pp. 7774-7778.
Holladay, et al., “Growth Hormone Conformation and Conformational Equilibria” Biochemistry, vol. 13, No. 8; 1974, pp, 1653-1661.
Holzman, et al., “Reoxidation of Reduced Bovine Growth Hormone From a Stable Secondary Structure” Biochemistry, vol. 25, No. 22; 1986, pp. 6907-6917.
Holzman, et al., “pH-Induced Conformational States of Bovine Growth Hormone” Biochemistry, vol. 29, No. 5; 1990, pp. 1255-1261.

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