The patent badge is an abbreviated version of the USPTO patent document. The patent badge does contain a link to the full patent document.

The patent badge is an abbreviated version of the USPTO patent document. The patent badge covers the following: Patent number, Date patent was issued, Date patent was filed, Title of the patent, Applicant, Inventor, Assignee, Attorney firm, Primary examiner, Assistant examiner, CPCs, and Abstract. The patent badge does contain a link to the full patent document (in Adobe Acrobat format, aka pdf). To download or print any patent click here.

Date of Patent:
Aug. 26, 2014

Filed:

May. 29, 2009
Applicants:

Gregory I. Frost, Del Mar, CA (US);

Anirban Kundu, San Diego, CA (US);

Louis H. Bookbinder, San Diego, CA (US);

Inventors:

Gregory I. Frost, Del Mar, CA (US);

Anirban Kundu, San Diego, CA (US);

Louis H. Bookbinder, San Diego, CA (US);

Assignee:

Halozyme, Inc., San Diego, CA (US);

Attorneys:
Primary Examiner:
Int. Cl.
CPC ...
C12N 9/24 (2006.01); C12P 21/06 (2006.01); C12N 15/00 (2006.01); C12N 1/20 (2006.01); C12N 5/00 (2006.01); C07H 21/04 (2006.01);
U.S. Cl.
CPC ...
Abstract

The invention relates to the discovery of novel Chondroitinase Glycoproteins (CHASEGPs), methods of manufacture, and potential uses in conditions where removal of chondroitin sulfates may be of therapeutic benefit. Chondroitinase Glycoproteins require both a substantial portion of the catalytic domain of the CHASEGP polypeptide and asparagine-linked glycosylation for optimal chondroitinase activity. The invention also includes carboxy-terminal deletion variants of CHASEGP that result in secreted variants of the protein to facilitate manufacture of a recombinant CHASEGP. Further described are suitable formulations of a substantially purified recombinant CHASEGP glycoprotein derived from a eukaryotic cell that generate the proper glycosylation required for its optimal activity. CHASEGP is useful for the degradation of glycosaminoglycans and chondroitin sulfate proteoglycans under clinical conditions where their removal is of therapeutic value.


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