Method of producing peptides or proteins as fusion proteins

Details Method of producing peptides or proteins as fusion proteins Method of producing peptides or proteins as fusion proteins

1994-05-16

1996-04-09

Draper, Garnette D.

Chemistry: molecular biology and microbiology

Micro-organism, tissue cell culture or enzyme using process...

Recombinant dna technique included in method of making a...

435 641, 4357523, 4353201, 435 693, 435 694, 435 696, 435 692, 435 695, 435 698, 536 234, C12N 1562

Patent

active

055061206

ABSTRACT:
A fusion protein comprising a carrier and a desired peptide or protein linked to the carrier via an enzymatically excisable dipeptide, such as Lys-Arg, is produced in a host microorganism and then the desired peptide or protein is recovered by treating the fusion protein at least with a protease specifically recognizing the dipeptide and specifically hydrolyzing the peptide bond of the dipeptide. The fusion protein includes tandem-form fusion proteins in which desired peptide or protein molecules are linked together repeatedly. According to the cleavage site in the dipeptide, the protease may be used in combination with an aminopeptidase specifically releasing a basic amino acid from the N-terminal side of the dipeptide and/or a carboxypeptidase specifically releasing a basic amino acid from the C-terminal side of the dipeptide.

REFERENCES:
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Gluschankof, et al., "Enzymes That Process Somatostatin Precursors", The Journal of Biological Chemistry, vol. 262, No. 20, pp. 9615-9620 (1987).
Sugimara, et al., "Purification, Characterization, and Primary Structure of Escherichia coli Protease VII with Specificity for Paired Basic Residues: Identity of Protease VII and OmpT", Journal of Bacteriology, vol. 170, No. 12, pp. 5625-5632 (1988).

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