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:
Mar. 17, 2020

Filed:

Feb. 23, 2018
Applicant:

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

Inventors:

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

Anirban Kundu, Georgetown, KY;

Gregory I. Frost, Palm Beach, FL (US);

Assignee:

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

Attorneys:
Primary Examiner:
Int. Cl.
CPC ...
A61K 38/47 (2006.01); A61K 45/06 (2006.01); C12N 9/26 (2006.01); A61K 47/68 (2017.01); A61K 47/60 (2017.01); A61K 39/395 (2006.01); A61K 35/768 (2015.01); A61K 38/46 (2006.01); C12N 7/00 (2006.01); A61K 39/00 (2006.01);
U.S. Cl.
CPC ...
A61K 47/6811 (2017.08); A61K 35/768 (2013.01); A61K 38/465 (2013.01); A61K 38/47 (2013.01); A61K 39/395 (2013.01); A61K 39/3955 (2013.01); A61K 47/60 (2017.08); C12N 7/00 (2013.01); C12N 9/2408 (2013.01); C12N 9/2474 (2013.01); A61K 2039/505 (2013.01); Y02A 50/466 (2018.01);
Abstract

The invention relates to the discovery of novel soluble neutral active Hyaluronidase Glycoproteins (sHASEGPs), methods of manufacture, and their use to facilitate administration of other molecules or to alleviate glycosaminoglycan associated pathologies. Minimally active polypeptide domains of the soluble, neutral active sHASEGP domains are described that include asparagine-linked sugar moieties required for a functional neutral active hyaluronidase domain. Included are modified amino-terminal leader peptides that enhance secretion of sHASEGP. The invention further comprises sialated and pegylated forms of a recombinant sHASEGP to enhance stability and serum pharmacokinetics over naturally occurring slaughterhouse enzymes. Further described are suitable formulations of a substantially purified recombinant sHASEGP glycoprotein derived from a eukaryotic cell that generate the proper glycosylation required for its optimal activity.


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