Search Patents
  • Patent number: 4996049
    Abstract: Treating composition and method for biological control of corn seed rots and seedling blights. The composition comprises a culture of emulsifier and surfactant producing bacteria selected from the strains of 6519EO1, 6133DO2, 6109DO1, and their respective genetic equivalents and a carrier. The composition is applied to seeds or the aqueous media surrounding seeds in plant growth media to prevent corn seed rot and seedling blight.
    Type: Grant
    Filed: December 19, 1988
    Date of Patent: February 26, 1991
    Assignee: Pioneer Hi-Bred International, Inc.
    Inventors: Douglas M. Haefele, Jonathan C. Lamptey, Joseph L. Marlow
  • Patent number: 6239101
    Abstract: Small, buffer soluble polypeptides having amino acid structures corresponding to residues 234-486, 310-486, and 407-486, of thrombomodulin and functionally equivalent analogs thereof inhibiting the clotting activity of thrombin and increasing protein C activation. The polypeptides can be coated onto the surface of articles adapted for contacting mammalian blood to render the surface non-thrombogenic. In pharmaceutical compositions, the polypeptides act as a natural anticoagulant.
    Type: Grant
    Filed: January 31, 1991
    Date of Patent: May 29, 2001
    Assignee: Oklahoma Medical Research Foundation
    Inventors: Charles T. Esmon, Naomi L. Esmon, Deborah J. Stearns, Shinichiro Kurosawa
  • Patent number: 5089605
    Abstract: The invention concerns unique immobilized immunoglobulin-binding protein materials which have a high binding capacity for immunoglobulins. Exemplified are preparations which have a high binding capacity for IgGl immunoglobulins. The preparations are made by covalently joining an immobilization support material to (a) an arginine-containing linker and (b) an immunoglobulin-binding protein material. The immunoglobulin-binding protein can be joined to the linker through an amide bond. Specifically disclosed is an immobilized protein A preparation. This immobilized protein A preparation has utility in the art of purifying monoclonal antibodies.
    Type: Grant
    Filed: March 13, 1987
    Date of Patent: February 18, 1992
    Assignee: Repligen Corporation
    Inventors: Albert T. Profy, Margaret A. Belew, Walter C. Herlihy
  • Patent number: 4981951
    Abstract: A method of purifying a recombinant protein from a solution, such as tissue culture fluid, containing gylcoproteins. The affinity of lectins for specific glycoproteins is assessed and used to select a particular lectin specific for the contaminating glycoprotein(s). A sugar buffer such as alpha methyl mannoside prevents binding of the recombinant protein. The preferred lectin is lentil lectin, for use in separating recombinant Factor VIII from tissue culture fluid contaminated with rodent protein from the cell line used to produce the recombinant Factor VIII.
    Type: Grant
    Filed: April 14, 1988
    Date of Patent: January 1, 1991
    Assignee: Miles Inc.
    Inventor: Grace C. Tsay
  • Patent number: 5260373
    Abstract: The invention concerns unique immobilized immunoglobulin-binding protein materials which have a high binding capacity for immunoglobulins. Exemplified are preparations which have a high binding capacity for IgGl immunoglobulins. The preparations are made by covalently joining an immobilization support material to (a) an arginine-containing linker and (b) an immunoglobulin-binding protein material. The immunoglobulin-binding protein can be joined to the linker through an amide bond. Specifically disclosed is an immobilized protein A preparation. This immobilized protein A preparation has utility in the art of purifying monoclonal antibodies.
    Type: Grant
    Filed: February 18, 1992
    Date of Patent: November 9, 1993
    Assignee: Repligen Corporation
    Inventors: Albert T. Profy, Margaret A. Belew, Walter C. Herlihy
  • Patent number: 5457048
    Abstract: The invention is directed to substantially purified Eph-related protein tyrosine kinases, or functional fragments thereof, having about 23 to 66 percent amino acid sequence identity in their carboxyl terminal variable regions compared to known members of the Eph subclass of tyrosine kinases. Nucleic acids encoding such Eph-related protein tyrosine kinases, vectors and host cells are also provided. The invention is also directed to a method of diagnosing cancer and determining cancer prognosis. The method includes removing a tissue or cell sample from a subject suspected of having cancer and determining the level of Eph-related protein tyrosine kinase in the sample, wherein a change in the level or activity of a Eph-related protein tyrosine kinase compared to a normal sample indicates the presence of a cancer or indicates the level of malignancy of a cancer.
    Type: Grant
    Filed: December 3, 1993
    Date of Patent: October 10, 1995
    Assignee: La Jolla Cancer Research Foundation
    Inventors: Elena B. Pasquale, Fereydoun G. Sajjadi
  • Patent number: 5187262
    Abstract: A cDNA clone (HEV1) encoding hevein was isolated via polymerase chain reaction (PCR) using mixed oligonucleotides corresponding to two regions of hevein as primers and a Hevea brasiliensis latex cDNA library as a template. HEV1 is 1018 nucleotides long and includes an open reading frame of 204 amino acids. The deduced amino acid sequence contains a puGOVERNMENT RIGHTSThis application was funded under Department of Energy Contract DE-AC02-76ER01338. The U.S. Government has certain rights under this application and any patent issuing thereon.
    Type: Grant
    Filed: September 24, 1990
    Date of Patent: February 16, 1993
    Assignee: Board of Trustees, operating Michigan State University
    Inventors: Natasha V. Raikhel, Willem F. Broekaert, Nam-Hai Chua, Anil Kush
  • Patent number: 5179196
    Abstract: The present invention provides a process for the recovery of heterologous proteins from CTAP-III fusion proteins comprising expressing a fusion protein having a first amino acid sequence, a second amino acid sequence, and a selectable site which may be cleaved to provide first and second polypeptide fragments, respectively, wherein the first amino acid fragment is homologous to CTAP-III, and the first and second fragments have different pI values; cleaving the fusion protein to provide the first and second fragments; and separating the first and second fragments by ion exchange chromatography.
    Type: Grant
    Filed: May 4, 1989
    Date of Patent: January 12, 1993
    Assignee: SRI International
    Inventors: Paul H. Johnson, Ping Sze, Richard C. Winant, Jerome B. Lazar
  • Patent number: 4973667
    Abstract: Nuclear polyhedrosis viruses, for example, Autographa californica nuclear polyhedrosis virus (AcMNPV), useful in the control of lepidopterous larvae such as the larvae of the cabbage looper Trichoplusia ni, have been found to have enhanced infectivity when mixed with certain proteins obtained from the granulin fraction of Trichoplusia ni granulosis virus (TnGV) or Heliothis armigera granulosis virus (HaGV), and from the polyhedrin fraction of AcMNPV viruses. The proteins from the TnGV granulin fraction have molecular weights of about 101 and about 104 kd. The enhanced infectivity is correlated to biochemical and structural changes in the T.ni peritrophic membrane.
    Type: Grant
    Filed: October 25, 1989
    Date of Patent: November 27, 1990
    Assignee: Boyce Thompson Institute for Plant Research, Inc.
    Inventor: Robert R. Granados
  • Patent number: 5677146
    Abstract: The present invention provides isolated DNA molecules comprising a DNA segment encoding a novel human amyloid protein precursor homologue and novel Kunitz-type inhibitors. Also provided are DNA constructs comprising a first DNA segment encoding a novel human amyloid protein precursor homologue or a novel Kunitz-type inhibitor wherein said first DNA segment is operably linked to additional DNA segments required for the expression for the first DNA segment, as well as host cells containing such DNA constructs and methods for producing proteins from the host cells.
    Type: Grant
    Filed: April 18, 1995
    Date of Patent: October 14, 1997
    Assignee: Zymogenetics, Inc.
    Inventors: Cindy A. Sprecher, Donald C. Foster, Kjeld E. Norris
  • Patent number: 5239056
    Abstract: A peptide fraction inducing the formation of antibodies which protect against the bovine leukemia virus (BLV), wherein it includes a peptide sequence which reproduces all or part of the sequence of the glycoprotein envelope gp51 fragment of the BLV virus which bears at least one of the epitopes (F, G, H) responsible for the biological activity of the virus. This fraction may be the fragment itself or a synthetic peptide. Application is made to the preparation or search for antibodies, to diagnosis and to the preparation of vaccines.
    Type: Grant
    Filed: February 5, 1992
    Date of Patent: August 24, 1993
    Assignee: Rhone Merieux
    Inventors: Daniel G. J. G. Portetellie, Arsene Leon G. Burny, Corine F. Dandoy, Helene S. C. Gras, nee Masse, Andre L. Tartar
  • Patent number: 5399494
    Abstract: Method of isolating deletion mutants of Vibrio cholerae, wherein the deletion is predetermined by digestion with restriction endonucleases of known specificity. The deletions are inserted into the Vibrio cholerae chromosome by in vivo recombination between a plasmid carrying the desired deletion, with adjacent flanking sequences, and the Vibrio cholerae chromosome. The invention includes the isolation and characterization of a new Vibrio cholerae strain, (ATCC No. 55456), having a deletion in the tox gene, as defined by Acc I, Xba I, Cla I and/or restriction endonuclease sites, and carrying a mercury resistance gene. The invention also includes vaccines for protecting against the symptoms of cholera as well as methods for achieving this protection.
    Type: Grant
    Filed: August 28, 1992
    Date of Patent: March 21, 1995
    Assignee: The University of Maryland System
    Inventors: James B. Kaper, Myron M. Levine
  • Patent number: 5464823
    Abstract: Peptide-based compounds containing four invariant cysteine residues which have been oxidized to obtain two intramolecular disulfide bonds are useful as preservatives and in preventing, treating, or ameliorating viral or microbial infection in animals and plants. These compounds, in one embodiment, are of the formula:A.sub.1 -A.sub.2 -A.sub.3 -A.sub.4 -A.sub.5 -C-A.sub.7 -C-A.sub.9 -A.sub.10 -A.sub.11 -A.sub.12 -C-A.sub.14 -C-A.sub.16 -(A.sub.17 -A.sub.18)(1) (SEQ ID NO:4)and the N-terminal acylated, C-terminal amidated or esterified and the cystine-bridged forms thereofwherein A.sub.1, A.sub.9, A.sub.10 and A.sub.11 are basic amino acids;A.sub.2 and A.sub.3 are small amino acids;A.sub.5, A.sub.7, A.sub.12, A.sub.14 and A.sub.16 are hydrophobic amino acids; andA.sub.4 is a basic or a small amino acid;A.sub.17 is not present or, if present, is a small amino acid;A.sub.18 is not present or, if present, is a basic amino acid.
    Type: Grant
    Filed: July 26, 1993
    Date of Patent: November 7, 1995
    Assignee: The Regents of the University of California
    Inventors: Robert I. Lehrer, Vladimir N. Kokryakov, Sylvia S. L. Harwig
  • Patent number: 5747452
    Abstract: The present invention provides fibronectin self-assembly sites. The invention provides a set of polypeptides derived from the first type III repeat of fibronectin which contain a fibronectin-fibronectin binding site. These polypeptides have been used to obtain a second set of polypeptides derived from the C-terminal type I repeats which contain a second fibronectin-fibronectin binding site which interacts with the first type III repeat of fibronectin. These polypeptides are capable of inhibiting fibronectin matrix assembly by interfering with fibronectin-fibronectin binding. These polypeptides are also capable of enhancing fibronectin matrix assembly and inducing disulfide cross-linking of fibronectin molecules in vitro. In addition, these polypeptides are capable of inhibiting migration of tumor cells. The polypeptides of the present invention have a number of related uses as well.
    Type: Grant
    Filed: June 1, 1995
    Date of Patent: May 5, 1998
    Assignee: La Jolla Cancer Research Foundation
    Inventors: Erkki I. Ruoslahti, Alex Morla
  • Patent number: 5099003
    Abstract: A method of preparing a sterile and stable plasma-protein solution containing fibrinogen and Factor XIII from human blood plasma which has been stabilized with citrate, comprising treating the plasma with .beta.-propiolactone and irradiating it with ultraviolet light, removing the Factors II, VII, IX and X by adsorption onto anion exchangers that adsorb proteins, precipitating the companion proteins out by adding ethanol until the solution has a final concentration of about 9% by volume at -3.degree. C., centrifuging the precipitate off, dissolving the precipitate in a citrate buffer at a pH of about 6.35 and a temperature of about 37.degree. C., adjusting the protein level of the solution to about 13.3 g/l with sodium citrate solution, adding ethanol, a glycine citrate buffer, and a solution of sodium citrate to precipitate out the companion proteins, adding ethanol to the remaining solution until the solution has a final concentration of about 9% by volume at -3.degree. C.
    Type: Grant
    Filed: October 12, 1988
    Date of Patent: March 24, 1992
    Assignee: Biotest Pharma GmbH
    Inventors: Ronald Kotitschke, Axel W. Stemberger, Wolfgang Stephan
  • Patent number: 5028694
    Abstract: A purified antigenic protein has been obtained which is capable of inducing in a chicken an immune response conferring protection against infection by Eimeria necatrix or Eimeria tenella. The protein has a molecular weight of about 26,000 and is composed of two polypeptides joined by a disulfide bond. The two polypeptide subunits have molecular weights of about 18,000 and about 8,000, respectively. The gene encoding the protein has been sequenced and the amino acid sequence of the protein deduced therefrom.The protein and antigenic polypeptides having an amino acid sequence included within the protein may be incorporated into a vaccine for conferring upon a chicken active immunity against infection by E. necatrix or E. tenella.
    Type: Grant
    Filed: December 3, 1985
    Date of Patent: July 2, 1991
    Assignee: Solvay & Cie, S.A.
    Inventors: Karel Z. Mewman, Jr., John L. Tedesco, Thomas C. Gore, Gary R. Petersen, Virginia M. Brothers, James G. Files, Leland S. Paul
  • Patent number: 5756465
    Abstract: There is disclosed an isolated polypeptide and derivatives thereof having protease biological activity for human precursor IL-1.beta. and for a substrate comprising:R.sub.1 -Asp-R.sub.2 -R.sub.3wherein R.sub.1 and R.sub.3 are independently any D or L isomer amino acid, R.sub.2 is Ala or Gly, and wherein the specific protease cleavage site is between Asp and R.sub.2. Inhibitor compounds, compositions and methods for inhibiting Interleukin 1.beta. protease activity are also disclosed. The inhibitor compounds comprise an amino acid sequence of from 1 to about 5 amino acids having an N-terminal blocking group and a C-terminal Asp residue connected to an electronegative leaving group, wherein the amino acid sequence corresponds to the sequence Ala-Tyr-Val-His-Asp.
    Type: Grant
    Filed: May 12, 1995
    Date of Patent: May 26, 1998
    Assignee: Sanofi
    Inventors: Paul R. Sleath, Roy A. Black, Shirley R. Kronheim
  • Patent number: 5003047
    Abstract: A method for purifying a biologically active ligate. In this method, a ligand bonded to a first phase and having a specific affinity for the ligate is provided. The ligate is provided with a second phase. The first and second phases are then contacted together under conditions in which the ligand and ligate form a complex bonded to the first phase, with the ligand and ligate held together only by one or more non-covalent pressure sensitive bonds. At least a part of the second phase is then separated from the first phase to provide a purified first phase, and the purified first phase subjected to a pressure of at least 300 atmospheres under conditions sufficient to cause release of the ligate from the complex, but not sufficient to cause significant release of the ligand from the first phase. These conditions do not irreversibly cause biological activity of the ligate to be significantly reduced.
    Type: Grant
    Filed: January 10, 1989
    Date of Patent: March 26, 1991
    Assignee: Massachusetts Institute of Technology
    Inventors: Martin L. Yarmush, William C. Olson
  • Patent number: 5066786
    Abstract: A method is described for the purification of crude human interferon from solutions containing it, which comprises:a) the complete adsorption of the crude interferon in a column of siliceous material which has previously been disinfected with an aqueous solution of formaldehyde;b) the washing of the column with non-pyrogenic, sterile, deionized water;c) the removal of the extraneous residual proteins by the elution of the column successively with a 1.4 M aqueous solution of NaCl in non-pyrogenic, sterile, deionized water, and with an aqueous solution of acetic acid having a molar concentration of 0.001 M to 0.003 M;d) the elution of the interferon from the column with an aqueous solution of acetic acid having a molar concentration of from 0.01 to 0.03 M and finally,e) the recovery and lyophilization of the elution containing the purified interferon.
    Type: Grant
    Filed: July 18, 1988
    Date of Patent: November 19, 1991
    Assignee: Sclavo, S.p.A.
    Inventors: Otello Protasi, Paolo Rappuoli
  • Patent number: 5393667
    Abstract: Eucaryotic NAD cyclases able to cause production of cyclic adenosine diphosphate ribose from nicotinamide adenine dinucleotide.
    Type: Grant
    Filed: February 22, 1993
    Date of Patent: February 28, 1995
    Inventors: Felix Strumwasser, Mark R. Hellmich
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