Abstract: A novel class of thermal hysteresis (antifreeze) proteins (THP) that have up to 100 times the specific activity of fish antifreeze proteins has been isolated and purified from the mealworm beetle, Tenebrio molitor. Internal sequencing of the proteins, leading to cDNA cloning and production of the protein in bacteria has confirmed the identity and activity of the 8.4 to 10.7 kDa THP. They are novel Thr- and Cys-rich proteins composed largely of 12-amino-acid repeats of cys-thr-xaa-ser-xaa-xaa-cys-xaa-xaa-ala-xaa-thr. At a concentration of 55 ?g/mL, the THP depressed the freezing point 1.6° C. below the melting point, and at a concentration of ˜1 mg/mL the THP or its variants can account for the 5.5° C. of thermal hysteresis found in Tenebrio larvae. The THP function by an adsorption-inhibition mechanism and produce oval-shaped ice crystals with curved prism faces.

Abstract: The present invention provides methods for determining the structure and/or function of one or more domains of a cation-dependent (and preferably calcium-dependent) polypeptide (particularly a calcium-dependent enzyme, which may be a protease such as calpain) in the presence of one or more cations. The invention further provides methods for identifying a ligand having the ability to bind to one or more ligand-binding domains (LBDs) of a cation-dependent (and preferably calcium-dependent) polypeptide, and ligands identified by these methods. The invention also provides methods of treating or preventing physical disorders in animals using these ligands.

Abstract: A novel class of thermal hysteresis (antifreeze) proteins (THP) that have up to 100 times the specific activity of fish antifreeze proteins has been isolated and purified from the mealworm beetle, Tenebrio molitor. Internal sequencing of the proteins, leading to cDNA cloning and production of the protein in bacteria has confirmed the identity and activity of the 8.4 to 10.7 kDa THP. They are novel Thr- and Cys-rich proteins composed largely of 12-amino-acid repeats of cys-thr-xaa-ser-xaa-xaa-cys-xaa-xaa-ala-xaa-thr. At a concentration of 55 &mgr;g/mL, the THP depressed the freezing point 1.6° C. below the melting point, and at a concentration of ˜1 mg/mL the THP or its variants can account for the 5.5° C. of thermal hysteresis found in Tenebrio larvae. The THP function by an adsorption-inhibition mechanism and produce oval-shaped ice crystals with curved prism faces.

Abstract: The present invention provides methods for determining the structure and/or function of one or more domains of a cation-dependent (and preferably calcium-dependent) polypeptide (particularly a calcium-dependent enzyme, which may be a protease such as calpain) in the presence of one or more cations. The invention further provides methods for identifying a ligand having the ability to bind to one or more ligand-binding domains (LBDs) of a cation-dependent (and preferably calcium-dependent) polypeptide, and ligands identified by these methods. The invention also provides methods of treating or preventing physical disorders in animals using these ligands.

Abstract: A novel class of thermal hysteresis (antifreeze) proteins (THP) that have up to 100 times the specific activity of fish antifreeze proteins has been isolated and purified from the mealworm beetle, Tenebrio molitor. Internal sequencing of the proteins, leading to cDNA cloning and production of the protein in bacteria has confirmed the identity and activity of the 8.4 to 10.7 kDa THP. They are novel Thr- and Cys-rich proteins composed largely of 12-amino-acid repeats of cys-thr-xaa-ser-xaa-xaa-cys-xaa-xaa-ala-xaa-thr. At a concentration of 55 &mgr;g/mL, the THP depressed the freezing point 1.6° C. below the melting point, and at a concentration of ˜1 mg/mL the THP or its variants can account for the 5.5° C. of thermal hysteresis found in Tenebrio larvae. The THP function by an adsorption-inhibition mechanism and produce oval-shaped ice crystals with curved prism faces.

Abstract: A novel class of thermal hysteresis (antifreeze) proteins (THP) that have up to 100 times the specific activity of fish antifreeze proteins has been isolated and purified from the mealworm beetle, Tenebrio molitor. Internal sequencing of the proteins, leading to cDNA cloning and production of the protein in bacteria has confirmed the identity and activity of the 8.4 to 10.7 kDa THP. They are novel Thr- and Cys-rich proteins composed largely of 12-amino-acid repeats of cys-thr-xaa-ser-xaa-xaa-cys-xaa-xaa-ala-xaa-thr. At a concentration of 55 &mgr;g/mL, the THP depressed the freezing point 1.6° C. below the melting point, and at a concentration of ˜1 mg/mL the THP or its variants can account for the 5.5° C. of thermal hysteresis found in Tenebrio larvae. The THP function by an adsorption-inhibition mechanism and produce oval-shaped ice crystals with curved prism faces.

Abstract: A novel method for the production of transgenic proteins of interest suitable for oral administration is disclosed. The method involves the preparation of a protein of interest suitable for oral administration within a non-food crop plant comprising, transforming the non-food crop plant with a suitable vector containing a gene of interest and appropriate regulatory regions to ensure expression of the gene of interest within the non-food crop plant, such that the non-food crop plant is characterized as being non-toxic, non-addictive, palatable, ad requiring minimal or no processing prior to oral administration. An example of a non-food crop plant is low lakaloid tobacco. Proteins of interest may include pharmaceutically active proteins such as growth regulators, insulin, interferons, interleukins, growth hormone, erythropoietin, G-CSF, GM-CSF, hPG-CSF, M-CSF, Factor VIII, Factor IX. tPA, antibodies, antigens and combinations and/or derivatives thereof.

Abstract: A novel class of thermal hysteresis, antifreeze proteins (THPs) has been isolated and purified from Choristoneura sp., including the eastern spruce budworm C. fumiferana. The invention provides for nucleic acids which encode these antifreeze proteins. The invention also provides for antibodies reactive to these novel antifreeze proteins. The invention also includes a method for decreasing the freezing point of an aqueous solution by adding these novel antifreeze proteins to the solution.

Abstract: A novel class of thermal hysteresis, antifreeze proteins (THPs) has been isolated and purified from Choristoneura sp., including the eastern spruce budworm C. fumiferana. The invention provides for nucleic acids which encode these antifreeze proteins. The invention also provides for antibodies reactive to these novel antifreeze proteins. The invention also includes a method for decreasing the freezing point of an aqueous solution by adding these novel antifreeze proteins to the solution.