DR. OSCAR L FRICK, MD
Medical Practice at Parnassus Ave, San Francisco, CA

7074900, Jul 11, 2006

Apr 23, 2003

10/422422

Bob B. Buchanan - Berkeley CA, US
Gregorio del Val - San Diego CA, US
Rosa M. Lozano - Madrid, ES
Joshua H. Wong - San Francisco CA, US
Boihan C. Yee - Walnut Creek CA, US
Oscar L. Frick - San Francisco CA, US

The Regents of the University of California - Oakland CA

C07K 14/00, C07K 14/415, A61K 39/35, A61K 39/36

530350, 530370, 530379, 514 2, 435 25, 435 681, 4241841, 4241851, 4242751, 426656, 426541

Thioredoxin, a small dithiol protein, is a specific reductant for allergenic proteins and particularly allergenic proteins present in pollen and animal and plant sources. All targeted proteins contain disulfide (S—S) bonds that are reduced to the sulfhydryl (SH) level by thioredoxin. The proteins are allergenically active and less digestible in the oxidized (S—S) state. When reduced (SH state), they lose their allergenicity and/or become more digestible. Thioredoxin achieved this reduction when activated (reduced) either by NADPH via NADP-thioredoxin reductase (physiological conditions) or by lipoic acid chemical reductant. Skin tests carried out with sensitized dogs showed that treatment of the pollens with reduced thioredoxin prior to injection eliminated or decreased the allergenicity of the pollen. Studies showed increased digestion of the pollen proteins by pepsin following reduction by thioredoxin. Pollen proteins that have been reduced by thioredoxin are effective and safe immunotherapeutic agents for decreasing or eliminating an animal's allergic reaction that would otherwise occur upon exposure to the non-reduced pollen protein.

2002015, Oct 17, 2002

Feb 2, 2001

09/776454

Gregorio Val - San Diego CA, US
Boihon Yee - Walnut Creek CA, US
Hye Jung - Alameda CA, US
Bob Buchanan - Berkeley CA, US
Oscar Frick - San Francisco CA, US

A61K049/00

424/009200, 800/003000

A method for testing the allergenicity of a heterologous protein produced by a plant or animal that has been genetically modified to produce that protein is disclosed. The method includes the steps of: (a) sensitizing a newborn dog from an atopic dog colony with a first extract prepared from tissue of the genetically modified plant or animal and containing a mixture of plant or animal proteins and the heterologous protein, by injecting or feeding the extract into the newborn dog; (b) after a period sufficient to allow the dog to establish an immune response to the sensitizing extract, challenging the dog with the extract; (c) observing the degree of allergic response provoked; (d) if a detectable skin reaction is observed, comparing the degree of skin reaction observed with that observed by carrying out steps (a)-(c) above, but where the sensitizing step (a) or applying step (b) is carried out with a second plant or animal extract containing substantially the same proteins as the first extract but lacking the heterologous protein; and (e) if the degree of skin reaction at (c) is greater than that observed by carrying out steps (a)-(c) in accordance with step (d), identifying the heterologous protein as a potential allergen in humans. Also disclosed is a dog for use in testing a biological substance for allergenicity in humans, and compositions useful in practicing the method.

6190723, Feb 20, 2001

Mar 23, 1998

9/046780

Bob B. Buchanan - Berkeley CA
Karoly Kobrehel - Montpellier, FR
Boihon C. Yee - Walnut Creek CA
Rosa Lozano - Madrid, ES
Oscar L. Frick - San Francisco CA
Richard W. Ermel - Winters CA

The Regents of the University of California - Berkeley CA

C07K 100

426656

Thioredoxin, a small dithiol protein, is a specific reductant for major allergenic proteins present in widely used foods from animal and plant sources. All targeted allergenic proteins contain disulfide (S--S) bonds that are reduced to the sulfhydryl (SH) level by thioredoxin. The proteins are allergenically active in the oxidized (S--S) state. When reduced (SH state), they lose their allergenicity. Thioredoxin achieved this reduction when activated (reduced) either by NADPH via NADP-thioredoxin reductase (physiological conditions) or by dithiothreitol, a chemical reductant. Skin tests and feeding experiments carried out with sensitized dogs showed that treatment of the food with reduced thioredoxin prior to ingestion eliminated or decreased the allergenicity of the food.

5792506, Aug 11, 1998

Oct 21, 1994

8/326976

Bob B. Buchanan - Berkeley CA
Karoly Kobrehel - Montpellier, FR
Boihon C. Yee - Walnut Creek CA
Rosa Lozano - Madrid, ES
Oscar L. Frick - San Francisco CA
Richard W. Ermel - Winters CA

The Regents of the University of California - Oakland CA

A23L 103

426656

Thioredoxin, a small dithiol protein, is a specific reductant for major allergenic proteins present in widely used foods from animal and plant sources. All targeted allergenic proteins contain disulfide (S--S) bonds that are reduced to the sulfhydryl (SH) level by thioredoxin. The proteins are allergenically active in the oxidized (S--S) state. When reduced (SH state), they lose their allergenicity. Thioredoxin achieved this reduction when activated (reduced) either by NADPH via NADP-thioredoxin reductase (physiological conditions) or by dithiothreitol, a chemical reductant. Skin tests and feeding experiments carried out with sensitized dogs showed that treatment of the food with reduced thioredoxin prior to ingestion eliminated or decreased the allergenicity of the food.

2006009, May 11, 2006

Sep 26, 2005

11/236012

Bob Buchanan - Oakland CA, US
Gregorio del Val - El Cerrito CA, US
Oscar Frick - San Francisco CA, US
Suzanne Teuber - Davis CA, US

The Regents of University of California - Oakland CA

A61K 39/00, G01N 33/53, A61K 39/35

424184100, 424275100, 435007100, 530370000

A 30 kDa ragweed complete pollen extract disulfide protein allergen has been purified from ragweed pollen. IgE immunoblots with sera of ragweed, walnut and ryegrass sensitive patients indicated that the 30 kDa protein is a major allergen. The 30 kDa protein finds use in allergy testing and immunotherapy regimens.

2003018, Sep 25, 2003

Feb 4, 2002

10/067620

Bob Buchanan - Berkeley CA, US
Gregorio del Val - San Diego CA, US
Oscar Frick - San Francisco CA, US
Suzanne Teuber - Dais CA, US

A61K049/00, A61K039/00

424/009810, 424/185100

A 30 kDa ragweed complete pollen extract disulfide protein allergen has been purified from ragweed pollen. IgE immunoblots with sera of ragweed, walnut and ryegrass sensitive patients indicated that the 30 kDa protein is a major allergen. The 30 kDa protein finds use in allergy testing and immunotherapy regimens.

2006009, Apr 27, 2006

Apr 11, 2003

10/510325

Bob Buchanan - Oakland CA, US
Peggy Lemaux - Moraga Town CA, US
Joshua Wong - San Francisco CA, US
Hyun-Kyung Kim - San Francisco CA, US
Oscar Frick - San Francisco CA, US

A01H 1/00, C12Q 1/68, C12N 5/04, C12N 15/82

800278000, 435006000, 435419000, 435468000

The selection of low allergen plant and animal subspecies, subgroups, and genotypes for production of low allergen food products is described.

2003017, Sep 11, 2003

Feb 4, 2002

10/067484

Bob Buchanan - Berkeley CA, US
Gregorio Val - San Diego CA, US
Oscar Frick - San Francisco CA, US

G01N033/53, G01N033/537, G01N033/543, A61K039/36, C07K014/415

435/007920, 424/185100, 424/275100, 530/379000

A 30 kDa ragweed complete pollen extract disulfide protein allergen has been purified from ragweed pollen. IgE immunoblots with sera of ragweed, walnut and ryegrass sensitive patients indicated that the 30 kDa protein is a major allergen. The 30 kDa protein finds use in allergy testing and immunotherapy regimens.