Bovine dipeptidylaminopeptidase 1

Details Bovine dipeptidylaminopeptidase 1 Bovine dipeptidylaminopeptidase 1

1998-04-03

2000-02-22

Hobbs, Lisa J.

Chemistry: molecular biology and microbiology

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

Enzymatic production of a protein or polypeptide

435212, 435219, 435272, C12P 2106, C12N 948, C12N 950, C07K 100

Patent

active

060279117

ABSTRACT:
The present invention provides the cDNA sequence encoding bovine dipeptidylaminopeptidase 1. The invention demonstrates that bovine DAP 1 coded by a single cDNA. The mature protein is derived from a single polypeptide consisting of a signal peptide, and a major polypeptide which is processed to generate the a subunit, b subunit and g subunit.

REFERENCES:
patent: 5126249 (1992-06-01), Becker, et al.
Paris, et al. "Molecular Cloning and Sequence Analysis of Human Preprocathespin C" FEBS Letters 369(2-3):326-330 (1995).
Lauritzen, et al. "BPTI and N-Terminal Extended Analogues Generated by Factor X.sub.a Cleavage and Cathespin C Trimming of a Fusion Protein Expressed in Escherichia coli" Protein Expression and Purification 2 (5/6):372-378 (Oct./Dec. 1991).
Smyth, et al. "Expression of recombinant Human Granzyme B.sup.1 : A Processing and Activation Role for dipeptidyl peptidase" Journal of Immunology 154(12):6299-6305 (Jun. 15, 1995).
Hutchinson, et al. "The preparation and properties of immobilised dipeptidyl-aminopeptidase I; (cathepspin C)" Biochimica et Biophysica Acta 916(1):1-4 (Nov. 5, 1987).

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