Queen's University at Kingston

Hsc Research Development Corporation

Seabright Corporation Limited

Peter L Davies

Virginia K Walker

Laurie A Graham

Yih-Cherng Liou

Mitra Rahavard

Michael G Tyshenko

Zongchao Jia

John S Elce

Christopher Hosfield

Tudor Moldoveanu

Garth Leonardo Fletcher

Choy Leong Hew

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,. 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 &#x3bc;g/mL, the THP depressed the freezing point 1.6&#xb0; C. below the melting point, and at a concentration of &#x2dc;1 mg/mL the THP or its variants can account for the 5.5&#xb0; C. of thermal hysteresis found inlarvae. The THP function by an adsorption-inhibition mechanism and produce oval-shaped ice crystals with curved prism faces.

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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.

Methods of determining polypeptide structure and function

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, . 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&deg; C. below the melting point, and at a concentration of &tilde;1 mg/mL the THP or its variants can account for the 5.5&deg; 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.

Tenebrio antifreeze proteins

A novel class of thermal hysteresis, antifreeze proteins (THPs) has been isolated and purified from Choristoneura sp., including the eastern spruce budworm . 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.

Spruce budworm antifreeze proteins, genes and method of using same

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.

Spruce budworm antifreeze proteins, genes and methods of using same

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Kingston, Canada

Peter L Davies