Altering protein functional properties through terminal fusions

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Blood proteins or globulins – e.g. – proteoglycans – platelet...

Reexamination Certificate

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C530S300000, C530S350000, C424S192100

Reexamination Certificate

active

10795062

ABSTRACT:
We disclose isolated terminal fusion polypeptides comprising a soybean glycinin or proglycinin polypeptide operably linked to the peptide of SEQ ID NO:12.

REFERENCES:
patent: 5710365 (1998-01-01), Kerr et al.
Utsumi et al., Structure-function Relationships of Soybean Proteins Revealed by Usining Recombinant Systems Enzyme and Microbial Technology, 2002, vol. 30, pp. 284-288.
Beardslee et al., Soybean Glycinin G1 Acidic Chain Shares IgE Epitopes with Peanut Allergen Ara h3 Allergy and Immunology, 2000, vol. 123, pp. 299-307.
Gidamis et al., Modification Tolerability of Soybean Proglycinin, Biosci, Biotech, Biochem. (1995) 59(8): 1593-1595.
Jung et al., Site-Specific Limited Proteolysis of Legumin Chlorampheniclo Acetyl Transferase Fusions in Vitro and In Transgenic Tobacco Seeds, Journal of Experimental Botany (1993) 44:343-349.
Kim et al., Improvement of nutritional value and funcation properties of soybean glycinin by protein engineering, Protein Enginerring (1990) 3(8):725-731.
Utsumi et al., Synthesis, processing and accumulationof modified glycinins of soybean in the seeds, leaves and stems of transgenic tobacco, Plant Science (1993) 92: 1991-202.
Utsumi et al., Effects of Deletion of Disulfide Bonds by Protein Engineering on the Confirmation and Functional Properties of Soybean Proglycinin, J. Agric. Food Chem. (1993) 41:687-691.
Utsumi et al., Structure-function relationships of soybean proteins revealed by using recombinant systems, Enzyme and Microbial Technology (2002) 30:284-288.

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