Fish; Fish Eggs; Shell Fish; Crustacea Patents (Class 530/857)
  • Patent number: 5523395
    Abstract: Disclosed are two lectin species isolated from the hemolymph of Japanese horseshoe crabs and Southern horseshoe crabs which bind to N-acetylneuraminic acid and N-glycolylneuraminic acid, but not to N-acetylglucosamine, glucoronic acid, or N-acetylgalactosamine.
    Type: Grant
    Filed: July 20, 1994
    Date of Patent: June 4, 1996
    Assignee: Maruha Corporation
    Inventors: Seiichi Ohkuma, Khomei Yanagi, Kuniharu Wada, Isami Tsuboi, Shoji Kimura, Masahito Matsukawa, Nobuyuki Sato
  • Patent number: 5484888
    Abstract: Gelatin, having high Bloom or gel strength in excess of 300, is extracted from fish, with high yield, by pre-treating collagen rich fish skins with a limewater (Ca(OH).sub.2) solution suspension with a concentration of between 19 gm of Ca(OH).sub.2 /liter of water/kg of tilapia fish skin to 100 gm Ca(OH).sub.2 /liter of water/kg of fish skin for a period of time between ten to sixty days and optimally between two to four weeks. For fish with higher percentage of fat content, a minimum concentration is at least 50 gm of Ca(OH).sub.2 /liter of water/kg of fish skin to avoid putrefaction. For fish with easily extractable gelatin, such as Nile perch, soaking time is from 3 to 10 days with a concentration of Ca(OH).sub.2 /liter of water of about 15 gm. At concentrations above 100 gm of Ca(OH).sub.2 /liter of water/kg of fish skin and/or treatment time periods in excess of four weeks, Bloom strength dramatically decreases.
    Type: Grant
    Filed: March 8, 1994
    Date of Patent: January 16, 1996
    Inventor: David Holzer
  • Patent number: 5420248
    Abstract: The present invention relates to the use of unpigmented skin from flat fish as novel industrial source of collagen. As unpigmented skin, the ventral skin is used in particular, from sole, dab, turbot, brill. Native acid-soluble collagen is advantageously extracted and separated by precipitation from the supernatant. The invention makes it possible to improve the collagen yield at reduced cost while preserving the native properties of the protein, and in a reproducible manner.
    Type: Grant
    Filed: January 4, 1994
    Date of Patent: May 30, 1995
    Assignee: Coletica
    Inventors: Pierre Devictor, Roland Allard, Eric Perrier, Alain Huc
  • Patent number: 5231011
    Abstract: The preparation of small peptides with multiple disulfide bonds is accomplished by forming a prepropeptide with an N-terminal excised region separated from the cysteine-rich peptide by one or more cleavable amino acid residues. The excised region preferably consists of an N-terminal end providing a hydrophobic signal sequence domain having up to approximately 25 amino acids, and an intermediate central propeptide domain having a variable length of between about 5-50 amino acids. The N-terminal excised region serves as a folding template to direct the formation of specific disulfide bonds in the cysteine-rich peptide. The cysteine-rich peptide is cleaved by enzymes releasing the biologically active peptide.
    Type: Grant
    Filed: April 18, 1991
    Date of Patent: July 27, 1993
    Assignee: University of Utah
    Inventors: David R. Hillyard, Baldomero M. Olivera
  • Patent number: 5229494
    Abstract: The present invention encompasses a receptor protein present on the surface of natural killer cells (NK cells) and non-specific cytotoxic cells (NCC) which is involved in non-specific lysis of target cells bearing an antigen recognized by the receptor protein and monoclonal antibodies which bind to the receptor which are useful in their identification and purification, and methods for altering NK cell-mediated lysis of target cells.The monoclonal antibodies (mAbs) of the present invention were prepared by cell fusions between spleen cells from mice immunized with either non-specific cytotoxic cells (NCC) from catfish (anti-receptor antibodies) and myeloma cells.The NK cell receptor was purified from solubilized flow cytometry purified non-specific cytotoxic (NCC) using antigen-antibody complexing techniques, either immune precipitation or affinity chromatography on Affigel-10.TM. with Con A Sepharose purified mAbs.
    Type: Grant
    Filed: December 3, 1990
    Date of Patent: July 20, 1993
    Assignees: University of Georgia Research Foundation, University of North Carolina
    Inventors: Donald L. Evans, David T. Harris
  • Patent number: 5185430
    Abstract: The present invention encompasses antigens recognized by the receptor protein, an antigen common to the surface of cells recognized and lysed by natural killer cells, monoclonal and heterologous antibodies which bind to the antigen proteins which are useful in their identification and purification, and methods for altering NK cell-mediated lysis of target cells.The monoclonal antibodies (mAbs) of the present invention were prepared by cell fusions between spleen cells from mice immunized with NC-37 human lymphoblastoid B-cells, which are susceptible to lysis by NK cells, and myeloma cells.The target cell antigen, a dimer of approximately 38,000 to 44,000 mw, seems to be evolutionarily conserved across species, from fish to mouse to man, an observation in agreement with the concept of NK cells being a primitive system, in terms of its appearance in evolution. The protein was purified from lysates of NC-37 cells by chromatography with mAbs bound to protein A beads followed by electrophoresis on 11% SDS-PAGE.
    Type: Grant
    Filed: August 9, 1990
    Date of Patent: February 9, 1993
    Assignees: University of Georgia Research Foundation, Inc., University of North Carolina
    Inventors: Donald L. Evans, David T. Harris
  • Patent number: 5162129
    Abstract: A particulate proteinaceous product and methods for producing the same from waste raw animal parts are disclosed. The product is dry to the touch, is compressible into pellets or cakes, and comprises about 45 to 65 w/w percent partially hydrolyzed, non-denatured animal protein, about 20-35 w/w percent oil derived from the animal parts, about 10-15 w/w percent moisture, and about 0-7 w/w percent ash. The product also has less objectionable odor, less propensity to oxidize, and higher nutritional value than existing products. The method involves mulling raw animal parts, hydrolyzing proteins in the animal parts with enzymes, heating to inactivate enzymes, screening, concentrating and adding oil, pasteurizing, removing water, separating oil and routing a portion of the separated oil to the beginning of concentrating as oil added. The method is distinctive in that it produces a dry, flaky product without the use of a conventional dryer.
    Type: Grant
    Filed: May 15, 1991
    Date of Patent: November 10, 1992
    Assignee: Advanced Hydrolyzing Systems, Inc.
    Inventors: Paul S. Anderson, Roger W. Law, Ronald R. Law, Kenneth Lum
  • Patent number: 5109111
    Abstract: Several known members of the corticotropin releasing factor (CRF) family have been synthesized and tested, including human and rat CRF which have the formula: H-Ser-Glu-Glu-Pro-Pro-Ile-Ser-Leu-Asp-Leu-Thr-Phe-His- Leu-Leu-Arg-Glu-Val-Leu-Glu-Met-Ala-Arg-Ala-Glu-Gln- Leu-Ala-Gln-Gln-Ala-His-Ser-Asn-Arg-Lys-Leu-Met-Glu- Ile-Ile-NH.sub.2. Peptides are herein disclosed that are potent competitive antagonists of CRF in mammals. One which has been found to be particularly potent is: H-D-Phe-His-Leu-Leu-Arg-Glu-Val-Leu-Glu-Nle-Ala- Arg-Ala-Glu-Gln-Leu-Ala-Gln-Gln-Ala-His-Ser-Asn- Arg-Lys-Leu-Nle-Glu-Ile-Ile-NH.sub.2. One that has shown particularly prolonged duration of potency is: H-D-Phe-His-Leu-Leu-Arg-Glu-Val-Leu-Glu-Nle-Ala- Arg-Ala-Glu-Gln-Leu-Ala-Gln-Gln-Ala-His-Ser-Asn- Arg-Lys-CML-Nle-Glu-Ile-Ile-NH.sub.2.
    Type: Grant
    Filed: March 23, 1990
    Date of Patent: April 28, 1992
    Assignee: The Salk Institute for Biological Studies
    Inventors: Jean E. F. Rivier, Wylie W. Vale, Jr., Catherine L. Rivier, Jean-Francois Hernandez
  • Patent number: 5093474
    Abstract: A process for the production of gelatin from fish skins comprises the steps of: (a) cleaning the skins in order to remove therefrom substantially all superfluous material; (b) treating with dilute aqueous alkali; (c) washing with water until the washing water is substantially neutral; (d) treating with dilute aqueous mineral acid; (e) washing with water until the washing water is substantially neutral; (f) treating with dilute aqueous citric acid and/or another suitable organic acid; (g) washing with water until the washing water is substantially neutral; and (h) extracting with water at elevated temperatures not above about 55.degree. c., the washed citric acid-treated skins. In practice, the present process employs much lower temperatures than known heretofore for the treatment steps, which results in a high quality product (e.g. absence of a fishy smell), compared with the prior art.
    Type: Grant
    Filed: April 12, 1989
    Date of Patent: March 3, 1992
    Assignee: Bar Ilan University
    Inventors: Shlomo Grossman, Margalit Bergman
  • Patent number: 5035896
    Abstract: According to this invention, the combination of a solid particulate water insoluble drug with a solid fish gelatin coating is produced by coacervation of the fish gelatin. The fish gelatin being soluble at ambient temperatures provides a basis for relatively low temperature coacervation impossible with other gelatins. Coacervation is brought about by the addition of conventional coacervation agents and the coacervating suspension containing gelatin and the agents is rendered insoluble by the addition of a suitable fixative such as glutaraldehyde.
    Type: Grant
    Filed: June 15, 1988
    Date of Patent: July 30, 1991
    Assignee: Warner-Lambert Company
    Inventors: Marilyn A. Apfel, Isaac Ghebre-Sellassie, Russell U. Nesbitt
  • Patent number: 4665158
    Abstract: Dehydrated protein materials are treated with gaseous HCl without temperature control, the reaction temperature being susceptible to reach, momentarily, 150.degree. C. Then the material thus treated is degassed and, after drying, a non hygroscopic powder usable in the food industry or in the pharmaceutical industry is obtained.
    Type: Grant
    Filed: May 30, 1985
    Date of Patent: May 12, 1987
    Assignee: Battelle Memorial Institute
    Inventors: Jean-Michel Armanet, Claude Giddey, Jean-Pierre Sachetto