IP Library Granted Patent US 11,530,238
Granted Patent B2
US 11,530,238 · App. 16/330,588 · Granted Dec 20, 2022

Methods for purifying antibodies

Inventors: Andre C. Dumetz (King of Prussia, PA); Kent E. Goklen (King of Prussia, PA); Nicholas E. Levy (King of Prussia, PA); Jessica Rachel Molek (King of Prussia, PA); Andrew S. Thomson (Collegeville, PA); Kenneth G. Yancey (Wayne, PA)
Assignee: GLAXOSMITHKLINE INTELLECTUAL PROPERTY DEVELOPMENT LIMITED
C07K1/22B01D15/3809B01D15/424C07K16/065
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Quick Facts
Patent No.
US 11,530,238
App. No.
16/330,588
Granted
Dec 20, 2022
Kind
B2
Abstract

The present invention relates to a method of purifying a recombinant polypeptide from Host Cell Proteins (HCP), the method comprising: (a) applying a solution comprising the recombinant polypeptide and HCP to a superantigen chromatography solid support, (b) washing the superantigen chromatography solid support with a wash buffer comprising caprylate and arginine; and (c) eluting the recombinant polypeptide from the superantigen chromatography solid support.

Claims (17)

1. A method of purifying a recombinant polypeptide from Host Cell Proteins (HCP), the method comprising: (a) applying a solution comprising the recombinant polypeptide and HCP to a superantigen chromatography solid support, (b) washing the superantigen chromatography solid support with a wash buffer comprising at least about 75 mM caprylate and greater than about 0.5 M arginine; and (c) eluting the recombinant polypeptide from the superantigen chromatography solid support.

2. The method according to claim 1 , wherein the caprylate is sodium caprylate.

3. The method according to claim 1 , wherein the wash buffer comprises about 75 mM to about 300 mM caprylate.

4. The method according to claim 1 , wherein the wash buffer comprises about 0.75 M to about 1.5 M arginine.

5. The method according to claim 1 , wherein the eluted recombinant polypeptide contains less than about 2% fragmented recombinant polypeptide.

6. The method according to claim 1 , wherein the HCP is derived from a mammalian cell.

7. The method according to claim 1 , wherein the HCP is phospholipase B-Like 2 protein.

8. The method according to claim 1 , wherein the HCP is cathepsin L.

9. The method according to claim 8 , wherein the purification of the recombinant polypeptide from cathepsin L is measured by a reduced cathepsin L activity in the eluate of step (c).

10. The method according to claim 1 , wherein the pH of the wash buffer is between pH 7 to pH 9.

11. The method according to claim 1 , wherein the recombinant polypeptide is a monoclonal antibody (mAb).

12. The method according to claim 11 , wherein the mAb is an IgG1, or an IgG4.

13. The method according to claim 1 , wherein the wash buffer does not contain sodium chloride.

14. The method according to claim 1 , wherein the superantigen is selected from the group consisting of Protein A, Protein G, and Protein L.

15. The method according to claim 1 , wherein after step (c) the amount of HCP is less than about 200 ng HCP/mg product.

16. A method of purifying a recombinant polypeptide from phospholipase B-Like 2 protein, the method comprising: (a) applying a solution comprising the recombinant polypeptide and phospholipase B-Like 2 protein to a superantigen chromatography solid support, (b) washing the superantigen chromatography solid support with a wash buffer comprising about 100 mM caprylate and about 1.1 M arginine; and (c) eluting the recombinant polypeptide from the superantigen chromatography solid support.

17. A method of purifying a recombinant polypeptide from cathepsin L, the method comprising: (a) applying a solution comprising the recombinant polypeptide and cathepsin L to a superantigen chromatography solid support, (b) washing the superantigen chromatography solid support with a wash buffer comprising about 150 mM caprylate and about 1.1 M arginine; and (c) eluting the recombinant polypeptide from the superantigen chromatography solid support.

Assignments (2)
CHANGE OF ADDRESS Recorded Oct 8, 2025
From: GLAXOSMITHKLINE INTELLECTUAL PROPERTY DEVELOPMENT LIMITED
To: GLAXOSMITHKLINE INTELLECTUAL PROPERTY DEVELOPMENT LIMITED
Reel/Frame 073032/0390 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Jul 14, 2021
From: DUMETZ, ANDRE C.; GOKLEN, KENT E.; LEVY, NICHOLAS E.; MOLEK, JESSICA RACHEL; THOMSON, ANDREW S.; YANCEY, KENNETH G.
To: GLAXOSMITHKLINE INTELLECTUAL PROPERTY DEVELOPMENT LIMITED
Reel/Frame 056857/0340 →
Continuity (2)
Provisional Application 62384240 · Sep 7, 2016
Related Publication 20210284686A1 · Sep 16, 2021
Cited By (1)
US 12,686,702