- Email: [email protected]
5202253 Monoclonal antibody specific for protein C and antibody purification method
131
PATENT ABSTRACTS restriction endonuclease from the fermented host which contains the plasmid encoding and expressing the Ncol restriction endonuelease activity.
5202253 MONOCLONAL ANTIBODY SPECIFIC FOR PROTEIN C AND ANTIBODY PURIFICATION METHOD Charles T Esmon, Naomi Esmon, Drongen, assigned to Oklahoma Medical Research Foundation A C a 2 + dependent monoclonal antibody that specifically binds to a specific twelve peptide sequence (E D Q V D P R L I D G K) in the activation region of the Protein C. The antibody does not bind to Activated Protein C and can be used to inhibit activation of Protein C by thrombin-thrombomodulin. The antibody can be isolated from cell culture or ascites fluid in large quantities by affinity chromatography with mild conditions using the peptide bound to an immobilized substrate. The antibody has a number of specific uses in isolation and characterization of Protein C and as a model for the design of C a 2 + dependent antibodies for the isolation of other proteins, as a diagnostic, and as a therapeutic to prevent activation of Protein C. The Protein C can be naturally produced or produced by expression of the recombinant gene. Advantages of the antibody in purification of Protein C include the specificity for Protein C and not Activated Protein C, and the unique Ca2+-peptide binding specificity which allows the binding site to be protected when it is being immobilized on the chromatographic support. In vivo, the antibody has been demonstrated to inhibit tumor growth. The antibody can also be used to promote clotting in patients having high levels of Factor VIII inhibitors.
that encode proteins having electrophysiological and pharmacological properties characteristic of glutamate receptors. The glutamate receptors are exemplified by proteins encoded by representative eDNA clones GhiRl, GIuR2, GIuR3, GhiR4, GIuR5, GIuR6 and GhiR7, fragments thereof, and functional combinations of these glutamate receptor proteins and/or fragments. D N A sequences from the eDNA clones for GIuRI, GIuR2, GIuR3, GIuR5 and GhiR5 are especially useful as probes, thus enabling those skilled in the art to identify, without undue experimentation, other members of the Lglutamate receptor family.
5202415 INSULIN
PRECURSORS
I Jonassen, Ib G Clausen, Einer B Jensen, Allan Svendsen, Drongen, assigned to Novo Nordisk A/S Insulin precursors characterized by the amino acid sequence B(1-29)-X1-X2-Y2-Y1-A(1-21), wherein B(1-29) are the 29 first amino acid residues of the B chain of human insulin starting from the N-terminus, A(i-21) are the 21 amino acid residues of the A chain of human insulin, X 1 represents a peptide bond or one or more arbitrary amino acid residues, X2 represents Ghi or Asp, and Y1 and Y2 each represents Lys or Arg, the positions A6 and A l l , A7 and B7 and A20 and B19, respectively, are connected through sulphur bridges, and, if desired, one or more of the amino acid residues of the chains B(1-29) and A(I-21) are substituted by another amino acid residue, are provided. The insulin precursors are prepared by culturing a yeast strain transformed with a replicable expression vehicle comprising a D N A sequence encoding an insulin precursor of the above formula in a suitable medium and isolating the insulin precursor thus formed from the culture medium. The insulin precursors can be converted into human insulin or insulin analogues by enzymatic treatment in a manner known per se.
5~22~ ISOLATED NUCLEIC ACIDS ENCODING GLUTAMATE RECEPTOR PROTEIN
5202419 ANTICOAGULATIVE PP4-X
PROTEIN
Stephen Heinemann, James Boulter, Michae Hollmann, Bernhar Bettler, Jan E Jensen, Drongen, assigned to The Salk Institute for Biological Studies
Ulrich Grundmann, Karl-Josef Abel, Egon Amann, Drongen, assigned to Behringwerke Aktiengesellsehaft
The present invention discloses novel DNAs
The protein PP4-X, whose amino acid sequence
PATENT ABSTRACTS restriction endonuclease from the fermented host which contains the plasmid encoding and expressing the Ncol restriction endonuelease activity.
5202253 MONOCLONAL ANTIBODY SPECIFIC FOR PROTEIN C AND ANTIBODY PURIFICATION METHOD Charles T Esmon, Naomi Esmon, Drongen, assigned to Oklahoma Medical Research Foundation A C a 2 + dependent monoclonal antibody that specifically binds to a specific twelve peptide sequence (E D Q V D P R L I D G K) in the activation region of the Protein C. The antibody does not bind to Activated Protein C and can be used to inhibit activation of Protein C by thrombin-thrombomodulin. The antibody can be isolated from cell culture or ascites fluid in large quantities by affinity chromatography with mild conditions using the peptide bound to an immobilized substrate. The antibody has a number of specific uses in isolation and characterization of Protein C and as a model for the design of C a 2 + dependent antibodies for the isolation of other proteins, as a diagnostic, and as a therapeutic to prevent activation of Protein C. The Protein C can be naturally produced or produced by expression of the recombinant gene. Advantages of the antibody in purification of Protein C include the specificity for Protein C and not Activated Protein C, and the unique Ca2+-peptide binding specificity which allows the binding site to be protected when it is being immobilized on the chromatographic support. In vivo, the antibody has been demonstrated to inhibit tumor growth. The antibody can also be used to promote clotting in patients having high levels of Factor VIII inhibitors.
that encode proteins having electrophysiological and pharmacological properties characteristic of glutamate receptors. The glutamate receptors are exemplified by proteins encoded by representative eDNA clones GhiRl, GIuR2, GIuR3, GhiR4, GIuR5, GIuR6 and GhiR7, fragments thereof, and functional combinations of these glutamate receptor proteins and/or fragments. D N A sequences from the eDNA clones for GIuRI, GIuR2, GIuR3, GIuR5 and GhiR5 are especially useful as probes, thus enabling those skilled in the art to identify, without undue experimentation, other members of the Lglutamate receptor family.
5202415 INSULIN
PRECURSORS
I Jonassen, Ib G Clausen, Einer B Jensen, Allan Svendsen, Drongen, assigned to Novo Nordisk A/S Insulin precursors characterized by the amino acid sequence B(1-29)-X1-X2-Y2-Y1-A(1-21), wherein B(1-29) are the 29 first amino acid residues of the B chain of human insulin starting from the N-terminus, A(i-21) are the 21 amino acid residues of the A chain of human insulin, X 1 represents a peptide bond or one or more arbitrary amino acid residues, X2 represents Ghi or Asp, and Y1 and Y2 each represents Lys or Arg, the positions A6 and A l l , A7 and B7 and A20 and B19, respectively, are connected through sulphur bridges, and, if desired, one or more of the amino acid residues of the chains B(1-29) and A(I-21) are substituted by another amino acid residue, are provided. The insulin precursors are prepared by culturing a yeast strain transformed with a replicable expression vehicle comprising a D N A sequence encoding an insulin precursor of the above formula in a suitable medium and isolating the insulin precursor thus formed from the culture medium. The insulin precursors can be converted into human insulin or insulin analogues by enzymatic treatment in a manner known per se.
5~22~ ISOLATED NUCLEIC ACIDS ENCODING GLUTAMATE RECEPTOR PROTEIN
5202419 ANTICOAGULATIVE PP4-X
PROTEIN
Stephen Heinemann, James Boulter, Michae Hollmann, Bernhar Bettler, Jan E Jensen, Drongen, assigned to The Salk Institute for Biological Studies
Ulrich Grundmann, Karl-Josef Abel, Egon Amann, Drongen, assigned to Behringwerke Aktiengesellsehaft
The present invention discloses novel DNAs
The protein PP4-X, whose amino acid sequence