Robert J Mccarthy

US Patent:

20030032146, Feb 13, 2003

Filed:

Jul 10, 2001

Appl. No.:

09/901996

Inventors:

Francis Dwulet - Greenwood IN, US
Neil Balgobin - Carmel IN, US
Robert McCarthy - Carmel IN, US

International Classification:

C12P021/04
C12P021/02
C07K001/22

US Classification:

435/069700, 530/413000, 435/068100, 530/344000

Abstract:

A hybrid polypeptide composed of an identification peptide and a desired functional protein are produced by recombinant DNA techniques. A DNA expression vector is constructed that includes segments of DNA coding for the identification peptide and the desired functional protein. The identification peptide consists of a specific sequence of amino acids that has the desired affinity for a non-antibody capture protein. This peptide maybe linked to either the amino or carboxyl terminal of the functional protein. The identification peptide may or may not contain a sequence of amino acids that can be fragmented by sequence specific proteases or chemical agents to yield the native protein. The hybrid polypeptide produced by either cell or cell-free based expression systems is now suitable for further processing. This fusion protein can be purified by affinity chromatographic techniques using an immobilized non-antibody capture protein that has the desired affinity for the identification peptide. Alternately the capture protein may contain a label that will allow for the tracking of the functional protein in the system being studied.

US Patent:

20040110255, Jun 10, 2004

Filed:

Sep 12, 2003

Appl. No.:

10/661207

Inventors:

Francis Dwulet - Greenwood IN, US
Neil Balgobin - Carmel IN, US
Robert McCarthy - Carmel IN, US

International Classification:

C12P021/04
C12N009/00

US Classification:

435/069700, 435/183000, 435/320100, 435/325000

Abstract:

A hybrid polypeptide composed of an identification peptide and a desired functional protein are produced by recombinant DNA techniques. A DNA expression vector is constructed that includes segments of DNA coding for the identification peptide and the desired functional protein. The identification peptide consists of a specific sequence of amino acids that has the desired affinity for a non-antibody capture protein. This peptide maybe linked to either the amino or carboxyl terminal of the functional protein. The identification peptide may or may not contain a sequence of amino acids that can be fragmented by sequence specific proteases or chemical agents to yield the native protein. The hybrid polypeptide produced by either cell or cell-free based expression systems is now suitable for further processing. This fusion protein can be purified by affinity chromatographic techniques using an immobilized non-antibody capture protein that has the desired affinity for the identification peptide. Alternately the capture protein may contain a label that will allow for the tracking of the functional protein in the system being studied.

US Patent:

20050214900, Sep 29, 2005

Filed:

Feb 23, 2005

Appl. No.:

11/063355

Inventors:

Francis Dwulet - Greenwood IN, US
Neil Balgobin - Carmel IN, US
Robert McCarthy - Carmel IN, US

International Classification:

C12P021/06

US Classification:

435068100

Abstract:

A hybrid polypeptide composed of an identification peptide and a desired functional protein are produced by recombinant DNA techniques. A DNA expression vector is constructed that includes segments of DNA coding for the identification peptide and the desired functional protein. The identification peptide consists of a specific sequence of amino acids that has the desired affinity for a non-antibody capture protein. This peptide maybe linked to either the amino or carboxyl terminal of the functional protein. The identification peptide may or may not contain a sequence of amino acids that can be fragmented by sequence specific proteases or chemical agents to yield the native protein. The hybrid polypeptide produced by either cell or cell-free based expression systems is now suitable for further processing. This fusion protein can be purified by affinity chromatographic techniques using an immobilized non-antibody capture protein that has the desired affinity for the identification peptide. Alternately the capture protein may contain a label that will allow for the tracking of the functional protein in the system being studied.

US Patent:

20100159564, Jun 24, 2010

Filed:

Dec 1, 2008

Appl. No.:

12/315237

Inventors:

Francis E. Dwulet - Greenwood IN, US
Andrew G. Breite - Fishers IN, US
Robert C. McCarthy - Carmel IN, US

International Classification:

C12N 9/52
C07H 21/04
C12N 5/10
C12N 5/071

US Classification:

435220, 536 232, 435325, 435381

Abstract:

The identification of the most sensitive sites of collagenase Class 1 to proteolysis by proteases present during the fermentation and purification of the enzyme is described. Culture supernatant obtained after fermentation of is used as the starting material for further purification of the enzyme. Native collagenase Class 1 and its proteolytic fragments are partially purified by a combination of hydrophobic interaction and strong anion exchange chromatographies. The pools containing enriched levels of the proteolytic fragments are further purified by high performance anion exchange chromatography. These polypeptides are then characterized by Q-TOF mass spectroscopy. A total of three sensitive bonds are identified along with substitution and deletion strategies that will result in resistance of the enzyme to proteolytic degradation.

US Patent:

49140400, Apr 3, 1990

Filed:

Mar 3, 1988

Appl. No.:

7/164054

Inventors:

Helmut Lenz - Tutzing, DE
Ellen Mossner - Tutzing, DE
Werner Stock - Grafelfing, DE
Albert Roder - Seeshaupt, DE
Harald Haug - Peissenberg, DE
Robert C. McCarthy - Carmel IN

Assignee:

Boehringer Mannheim GmbH - Mannheim

International Classification:

C01N 100
C01N 33503
C01N 3353

US Classification:

436175

Abstract:

The invention teaches a method for improving the ability to determine a polyvalent substance via use of an immunoaggregate during the assay. The immunoaggregate eliminates substances which can lead to incorrect results otherwise.