The United States of America As Represented by the Department of Health

The United States of America, As Represented by the Secretary, Department of Health and Human Services

East Carolina University

Enzon, Inc.

Brian M Martin

Edward J Ginns

Robert G Shorr

Carl W Gilbert

Myung-Ok Cho

William K Eliason

Kara A Maysak

Mary E LaMarca

Edward I Ginns

Dean D Metcalfe

Paul L Fletcher

Pillarisetti V Roa

Maryann D Fletcher

The present invention relates to metalloprotease enzymes isolated from scorpion venom, their nucleic acid and amino acid sequences, and methods of use thereof in the treatment of various diseases, disorders and cosmetic conditions.

Fast acting SNARE-cleaving enzymes

Glucocerebrosidase produced by recombinant methods and having use for treatment of Gaucher's disease is disclosed. A cDNA for encoding the specific protein is taught along with the method of preparing the construct used to produce the protein.

Cloned DNA for synthesizing unique glucocerebrosidase

The invention is directed to a pharmaceutical composition comprising a therapeutic amount of a glycosylated recombinantly-produced human glucocerebrosidase protein in a pharmaceutically acceptable carrier. The invention is further directed to a method of treating Gaucher's disease comprising administering to a subject afflicted with Gaucher's disease a therapeutic amount of a pharmaceutical composition comprising a therapeutic amount of a glycosylated recombinantly-produced human glucocerebrosidase protein in a pharmaceutically acceptable carrier.

Conjugates containing glucocerebrosidase and non-antigenic polymers such as polyethylene glycol are disclosed. The conjugates circulate for extended times and have prolonged activity in vivo when compared to unmodified enzymes. The conjugates are useful in the treatment of Gaucher's Disease and have improved enzyme activity at the pH ranges associated with lysosomal, arterial and capillary regions.

Glycolipid enzyme-polymer conjugates

A major heat-stable shrimp allergen is characterized as a 34 kDa protein corresponding to shrimp tropomyosin. Two IgE binding epitopes of this allergen have the sequences FLAEEADRK (SEQ ID NO: 1) and MQQLENDLDQVQESLLK (SEQ ID NO: 2), respectively. Surprisingly, both antigenic and allergenic activities of the allergen were found to be associated with these two peptide fractions. A-a-id antibodies recognized this allergen as well as a homologous 34 kDa allergen from lobster, prawn and crab, indicating that these antibodies recognize major cross-reacting IgE binding epitopes common to crustacea. The two epitopes are useful in the diagnosis and/or treatment of allergies, particularly in the desensitization of individuals that are allergic to shrimp and other crustacea. Variants and subfragments of the two epitopes display allergenicity, as assessed by reaction with allergen-specific IgE obtained from shrimp-sensitive patients.

IgE-binding epitopes of a major heat-stable crustacean allergen derived

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Rockville, MD, United States of America

Brian M Martin