Patents Examined by Gabriele E. Bugaisky
  • Patent number: 5595972
    Abstract: The invention is directed to A-lineage conotoxin peptides, which are conotoxin peptides that have strong homology in the signal sequence and the 3'-untranslated region of the genes coding for these peptides to the sequences in the .alpha.-conotoxin peptides. The A-lineage conotoxin peptides include the .alpha.-conotoxin peptides, the .alpha.-conotoxin-like peptides and the .kappa.-conotoxin peptides, described further below. The .alpha.-conotoxin-peptides generally share a "core" sequence motif. This core sequence is termed the .alpha.3/5 core and is represented as Cys-Cys-Xaa-Xaa-Xaa-Cys-Xaa-Xaa-Xaa-Xaa-Xaa-Cys (SEQ ID NO: 1). The .alpha.-conotoxin-like peptides generally share a core sequence termed the .alpha.4/7 core and is represented as Cys-Cys-Xaa-Xaa-Xaa-Xaa-Cys-Xaa-Xaa-Xaa-Xaa-Xaa-Xaa-Xaa-Cys (SEQ ID NO:2). The .kappa.-conotoxin peptides generally have a core sequence termed the .kappa.
    Type: Grant
    Filed: June 7, 1995
    Date of Patent: January 21, 1997
    Assignee: University of Utah Research Foundation
    Inventors: Baldomero M. Olivera, Lourdes J. Cruz, David R. Hillyard, J. Michael McIntosh, Ameurfino D. Santos
  • Patent number: 5589359
    Abstract: Chimeric proteins possessing Kunitz-type domain 1 of TFPI-2 and Kunitz-type domain 2 of TFPI are disclosed, as are muteins of TFPI and TFPI-2. Nucleic acid sequences, expression vectors and transformed host cells encoding and capable of producing the disclosed chimeric proteins and muteins are also disclosed. Finally, methods for prevention and treatment of septic shock using the chimeric proteins and muteins are disclosed.
    Type: Grant
    Filed: August 5, 1994
    Date of Patent: December 31, 1996
    Assignee: Chiron Corporation
    Inventors: Michael A. Innis, Abla A. Creasey
  • Patent number: 5589384
    Abstract: A fusion protein suitable for use as a vaccine comprises an amino acid sequence having biological activity which is fused via an intervening hinge comprising from two to eight glycine-proline repeats to the C-terminus of sufficient of the amino acid sequence of a B subunit of an enterotoxin which is capable of ADP-ribosylation of a GTPase.
    Type: Grant
    Filed: May 2, 1994
    Date of Patent: December 31, 1996
    Assignee: Glaxo Wellcome Inc.
    Inventors: Martin J. Lipscombe, Ian G. Charles, Neil F. Fairweather
  • Patent number: 5587311
    Abstract: The invention relates to antigens derived from ticks and to their purification. It also relates to genes encoding such antigens and to their cloning and expression from recombinant DNA molecules. Further, the invention describes the use of purified antigens and recombinant expression products having similar biological activity to those purified antigens to provide vaccines to protect cattle against tick infestation.
    Type: Grant
    Filed: October 19, 1994
    Date of Patent: December 24, 1996
    Assignees: Biotechnology Australia Pty. Ltd., Commonwealth Scientific and Industrial Research Organization
    Inventors: Gary S. Cobon, Joanna T. Moore, Law A. Y. Johnston, Peter Willadsen, David H. Kemp, Alagacone Sriskantha, George A. Riding, Keith N. Rand
  • Patent number: 5583016
    Abstract: Nucleic acids comprising the RNA component of a mammalian telomerase are useful as pharmaceutical, therapeutic, and diagnostic reagents.
    Type: Grant
    Filed: October 27, 1994
    Date of Patent: December 10, 1996
    Assignee: Geron Corporation
    Inventors: Bryant Villeponteau, Junli Feng, Walter Funk, William H. Andrews
  • Patent number: 5583030
    Abstract: The invention provides the LCB1 and LCB2 genes of the yeast Saccharomyces cerevisiae that encode subunits of the enzyme serine palmitoyltransferase (SPT), the first enzyme leading to synthesis of the long-base component of the sphingolipids. The present specification describes the isolation of the LCB1 and LCB2 genes. The invention further relates to methods of using these genes to either inhibit SPT activity or to inhibit synthesis of the enzyme. Furthermore, the invention relates to methods for constructing strains of S. cerevisiae or other organisms that can be used to select and to test for compounds that either inhibit SPT activity or to inhibit synthesis of the enzyme.
    Type: Grant
    Filed: December 28, 1994
    Date of Patent: December 10, 1996
    Assignee: The University of Kentucky Research Foundation
    Inventors: Robert C. Dickson, Robert L. Lester
  • Patent number: 5578480
    Abstract: This invention relates to methods for the isolation and purification of the recombinantly expressed major protein component of chondroitinase ABC, which is referred to as "chondroitinase I", from Proteus vulgaris (P. vulgaris). This invention further relates to methods for the isolation and purification of the recombinantly expressed second protein component of chondroitinase ABC, which is referred to as "chondroitinase II", from P. vulgaris. These methods provide significantly higher yields and purity than those obtained by adapting for the recombinant enzymes the method previously used for isolating and purifying native chondroitinase I enzyme from P. vulgaris.
    Type: Grant
    Filed: April 22, 1994
    Date of Patent: November 26, 1996
    Assignee: American Cyanamid Company
    Inventor: Kiran M. Khandke
  • Patent number: 5550046
    Abstract: A protein having an .alpha.-glucosidase activity, wherein its N-terminal amino acid sequence is the sequence depicted in the Sequence Listing of the present invention at Sequence No: 1; a DNA having the genetic information of the protein having an .alpha.-glucosidase activity; a recombinant vector containing said DNA; a transformant transformed with said vector; and production of .alpha.-glucosidase comprising culture of said transformant in a medium so as to grow .alpha.-glucosidase, and harvesting said .alpha.-glucosidase. According to the present invention, .alpha.-glucosidase without contamination of amylase can be easily produced in high yields and in large amounts by genetic engineering.
    Type: Grant
    Filed: March 22, 1993
    Date of Patent: August 27, 1996
    Assignee: Toyo Boseki Kabushiki Kaisha
    Inventors: Yuzuru Suzuki, Yukio Takii, Kazumi Yamamoto, Yoshiaki Nishiya, Atsushi Sogabe, Yukihiro Sogabe, Shigenori Emi
  • Patent number: 5476926
    Abstract: Regulatory DNA sequences are provided, which are obtained from the 5' flanking region of genes which are expressed primarily in differentiated adipose tissue. These DNA sequences are largely responsible for driving the expression of endogenous genes specifically in adipose tissue in vivo. The DNA sequences can be located in a region 5' of the gene, distinct from promoter sequences which provide a site for the initiation of transcription into DNA, or can be located within the region of the promoter itself.When operatively linked to a gene encoding a recombinant protein capable of exerting an effect on the metabolism of adipocytes, the DNA sequences of the invention can be used to produce transgenic animals which exhibit altered fat tissue metabolism. Depending upon the nature of the gene introduced in the animal or ancestor thereof at an embryonic stage, the transgenic animals are leaner or more obese than non-transgenic animals of the same species.
    Type: Grant
    Filed: October 7, 1991
    Date of Patent: December 19, 1995
    Inventors: Bruce M. Spiegelman, Reed Graves, Susan Ross
  • Patent number: 5470825
    Abstract: Several natural polypeptides (basophil granule proteins, "BGP") derived from the cytoplasmic granules of human basophils, and modified forms thereof, are described. These polypeptides, the DNA which encodes them and antibodies which recognize them, are useful as diagnostics for, and treatments for, pathologies involving inflammatory and IgE-mediated responses, parasitic and helminthic infections, hypersensitivity reactions and certain types of leukocytic leukemias.
    Type: Grant
    Filed: June 15, 1994
    Date of Patent: November 28, 1995
    Assignee: Incyte Pharmaceuticals, Inc.
    Inventors: Randy W. Scott, Gerald J. Gleich, Craig G. Wilde
  • Patent number: 5443966
    Abstract: The present invention relates to an expression vector encoding mature fragment C of tetanus toxin. The invention further relates to an E. coli host transformed by that vector and to a process for producing mature fragment C of tetanus toxin using same.
    Type: Grant
    Filed: August 23, 1993
    Date of Patent: August 22, 1995
    Inventors: Neil F. Fairweather, Andrew J. Makoff
  • Patent number: 5432070
    Abstract: The invention concerns a DNA which codes for a protein with N-methylhydantoinase activity and which has1.) the nucleic acid sequence shown in FIG. (1),2.) a sequence corresponding to it within the scope of the degeneracy of the genetic code or(3) a sequence which hybridizes with a sequence from (1) or/and (2) under stringent conditions.Furthermore the invention also concerns a recombinant vector which contains a DNA according to the present invention, a cell which is transformed with a vector according to the present invention as well as a process for producing a recombinant protein with NMHase activity.
    Type: Grant
    Filed: June 10, 1994
    Date of Patent: July 11, 1995
    Assignee: Boehringer Mannheim GmbH
    Inventors: Gunther Schumacher, Helmut Burtscher, Hans Mollering
  • Patent number: 5372928
    Abstract: Two new isolates of the Hepatitis C virus (HCV), J1 and J7, are disclosed. These new isolates comprise nucleotide and amino acid sequences which are distinct from the prototype HCV isolate, HCV1. Thus, J1 and J7 provide new polynucleotides and polypeptides for use, inter alia, in diagnostics, recombinant protein production and vaccine development.
    Type: Grant
    Filed: February 24, 1994
    Date of Patent: December 13, 1994
    Assignees: Chiron Corporation, The Director General of the National Institute of Health of Japan
    Inventors: Tatsuo Miyamura, Izumi Saito, Michael Houghton, Amy J. Weiner, Jang Han, Janice A. Kolberg, Tai-An Cha, Bruce D. Irvine
  • Patent number: 5362490
    Abstract: The present invention relates to a novel human interferon-gamma derived from an established human myelomonocyte, a process to prepare said interferon-gamma, and its use. The human myelomonocyte interferon-gamma has a novel polypeptide and carbohydrate chain structure, and it is effective in preventing and treating viral diseases, malignant tumors and immunopathies alone or in combination with other lymphokine and/or chemotherapeutic.
    Type: Grant
    Filed: May 17, 1993
    Date of Patent: November 8, 1994
    Assignee: Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo
    Inventors: Masashi Kurimoto, Masakazu Mitsuhashi
  • Patent number: 5317085
    Abstract: This invention relates to the identification, characterization, and sequencing of genetic sequences of human secretory granule proteoglycan peptide core protein, recombinant DNA clones directed against this sequence and against the sequence of the antisense RNA, and antibodies which recognize the native human secretory granule proteoglycan.
    Type: Grant
    Filed: July 7, 1992
    Date of Patent: May 31, 1994
    Assignee: Brigham And Women's Hospital
    Inventors: Richard L. Stevens, John H. Weis, Christopher F. Nicodemus
  • Patent number: 5306616
    Type: Grant
    Filed: June 6, 1991
    Date of Patent: April 26, 1994
    Assignee: Baylor College of Medicine
    Inventors: James R. Lupski, Pragna I. Patel, Roberto M. de Oca-Luna, Odila S. Cardenas
  • Patent number: 5288639
    Abstract: A polypeptide sequence from Candida albicans is described which has significant sequence homology with known stress proteins from other organisms, particularly the heat shock protein hsp 90 of Sacchromyces cerevisiae. Corresponding DNA sequences are also described, together with antibodies raised against fragments of the sequence. The polypeptide and DNA sequences and antibodies provide separate means for the diagnosis and/or treatment of fungal, particularly Candida, infections.
    Type: Grant
    Filed: March 14, 1991
    Date of Patent: February 22, 1994
    Assignee: The Victoria University of Manchester
    Inventors: James P. Burnie, Ruth C. Matthews
  • Patent number: 5278062
    Abstract: This disclosure relates to a novel class of serine proteases isolated from a culture medium of fungus Tritirachium album. The serine proteases disclosed have a high degree of stability in detergent formulations.In addition, this disclosure relates to a process for producing such serine proteases using recombinant techniques.
    Type: Grant
    Filed: May 1, 1992
    Date of Patent: January 11, 1994
    Assignee: Amgen
    Inventors: Babru B. Samal, Yitzhak Stabinsky
  • Patent number: 5272254
    Abstract: DNA sequences, hybrid DNA sequences, recombinant DNA molecules and processes for producing streptavidin-like polypeptides and for producing fused proteins consisting of a streptavidin-like polypeptide joined end to end with another protein, polypeptide, peptide or amino acid. The DNA sequences, hybrid DNA sequences and recombinant DNA molecules of this invention are characterized in that they include DNA fragments that code for streptavidin-like polypeptides. These DNA sequences, hybrid DNA sequences and recombinant DNA molecules and the hosts transformed with them may be employed in the processes of this invention to produce streptavidin-like polypeptides and fused proteins.
    Type: Grant
    Filed: November 27, 1991
    Date of Patent: December 21, 1993
    Assignee: Biogen Inc.
    Inventors: Harry M. Meade, Jeffrey L. Garwin
  • Patent number: 5270181
    Abstract: This invention provides a fusion molecule comprising a DNA sequence encoding a thioredoxin-like protein fused to the DNA sequence encoding a selected heterologous peptide or protein. The peptide or protein may be fused to the amino terminus of the thioredoxin-like molecule, the carboxyl terminus of the thioredoxin-like molecule, or within the thioredoxin-like molecule, for example at the active-site loop of said molecule. Expression of this fusion molecule under the control of a regulatory sequence capable of directing its expression in a desired host cell, produces high levels of stable and soluble fusion protein. The fusion protein, located in the bacterial cytoplasm, may be selectively released from the cell by osmotic shock or freeze/thaw procedures. It may be optionally cleaved to liberate the soluble, correctly folded heterologous protein from the thioredoxin-like portion.
    Type: Grant
    Filed: August 14, 1991
    Date of Patent: December 14, 1993
    Assignee: Genetics Institute, Inc.
    Inventors: John McCoy, Edward R. LaVallie