Arthur L Haas

US Patent:

59860804, Nov 16, 1999

Filed:

Oct 17, 1997

Appl. No.:

8/954333

Inventors:

Ikuko Masuda - Wauwatosa WI
Joseph T. Barbieri - New Berlin WI
Arthur L. Haas - Brookfield WI
Brian D. Halligan - Wauwatosa WI
Daniel J. McCarty - Hartland WI
Lawrence M. Ryan - Wauwatosa WI

Assignee:

MCW Research Foundation - Milwaukee WI

International Classification:

C07N 2104
C12N 914
C12N 120
C12N 1500

US Classification:

536 232

Abstract:

We have cloned and sequenced the cDNA encoding the 61 kD active fragment of a unique porcine chondrocyte nucleotide pyrophosphohydrolase (NTPPHase) from a porcine chondrocyte library. Degenerate oligonucleotides, corresponding to the N-terminal amino acid sequence of this peptide were hybridized to porcine chondrocyte cDNA and used to amplify DNA encoding the N-terminal sequence of 61 kD with the polymerase chain reaction (PCR). The PCR products were then used as probes to clone the entire open reading-frame for the 61 kD fragment from a porcine chondrocyte cDNA library. The length of the cloned cDNA was 2509 bp. Translation of the open-reading-frame predicts the 61 kD fragment to be a 459 amino acid protein. BLAST and FASTA analysis confirmed that this amino acid sequence was unique and did not possess high homology to any known proteins in the non-redundant protein data base. Limited homology (17%) between the 61 kD fragment and several prokaryotic and eukaryotic ATP pyrophosphate-lyase (adenylate cyclase) was detected.

US Patent:

57143471, Feb 3, 1998

Filed:

Dec 22, 1995

Appl. No.:

8/577640

Inventors:

Arthur L. Haas - Brookfield WI
Jana Narasimhan - Wauwatosa WI

Assignee:

MCW Research Foundation - Milwaukee WI

International Classification:

C12N 1512
C07K 1447

US Classification:

435 691

Abstract:

A method of preparing recombinant ubiquitin cross-reactive protein (UCRP) is disclosed. In one embodiment, the method comprises the step of purifying UCRP from a host cell in the presence of a cobalt or Group IIb metal, wherein the cobalt or Group IIb metal prevents proteolytic inactivation of UCRP occurring by cleavage of the UCRP carboxyl terminal glycine dipeptide. In another embodiment the method comprises purifying UCRP comprising an additional arginine or lysine residue at the carboxy terminal. A preparation of UCRP with an additional arginine residue at the carboxy terminus is also disclosed.

US Patent:

20160201049, Jul 14, 2016

Filed:

Mar 31, 2016

Appl. No.:

15/086719

Inventors:

Arthur L. Haas - New Orleans LA, US
Virginia P. Ronchi - New Orleans LA, US

Assignee:

Board of Supervisors of Louisiana State University and Agricultural and Mechanical College - Baton Rouge LA

International Classification:

C12N 9/00

Abstract:

Methods are provided for modulating the activity of multimeric ubiquitin-protein E3 ligases including, but not limited to, E6AP ligase activities. The methods reduce the level of oligomer formation such as homotrimeric E6AP ligase to reduce the enzyme activity. Alternatively, agents are provided that can promote the association of the ligase monomers, thereby increasing the ligase activity. Accordingly, novel therapeutic strategies are provided that are useful for the treatment of pathologies resulting from mutations in the genes encoding the ligases and which adversely increase or decrease a ubiquitination reaction.

US Patent:

20150210998, Jul 30, 2015

Filed:

Apr 14, 2015

Appl. No.:

14/685865

Inventors:

Arthur L. Haas - New Orleans LA, US
Virginia P. Ronchi - New Orleans LA, US

Assignee:

Board of Supervisors of Louisiana State University and Agricultural and Mechanical College - Baton Rouge LA

International Classification:

C12N 9/99

Abstract:

Methods are provided for modulating the activity of multimeric ubiquitin-protein E3 ligases including, but not limited to, E6AP ligase activities. The methods reduce the level of oligomer formation such as homotrimeric E6AP ligase to reduce the enzyme activity. Alternatively, agents are provided that can promote the association of the ligase monomers, thereby increasing the ligase activity. Accordingly, novel therapeutic strategies are provided that are useful for the treatment of pathologies resulting from mutations in the genes encoding the ligases and which adversely increase or decrease a ubiquitination reaction.