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5175252 Cloned gene encoding for bacteriocin from pediococcus acidilactici
New Patents
for DNA sequencing and as hybridization probes, linkers and adapters in the cloning of genes.
5175252 CLONED GENE ENCODING FOR BACTERIOCIN FROM PEDIOCOCCUS ACIDILACTICI John D Marugg, Adrianus M Ledeboer, Peter A Vandenbergh, James Henderson, Utrecht, FL, Netherlands assigned to Quest International Flavors & Food Ingredients Co Isolation and identification of a gene encoding for a bacteriocin precursor in Pediococcus acidilactici, cloning of the gene in a vector plasmid and transformation to bacteria is described. The bacteriocin is particularly useful for inhibiting Listeria in food products.
ix
5175267 STEREOSELECTIVE GLYCOSYLATION OF HETERCYCLIC BASES Chung K Chu assigned to University of Georgia Research Foundation Inc A method of preparation of 2’,3’-dideoxy and 2’,3’-dideoxy-2, 3’-didehydronucleosides that includes the step of condensing a l-O-activated2-(aromatic or aliphatic)-selenenyl-5-0 protected ribose with a protected heterocyclic base in the presence of trimethybilyl triflate or a Lewis acid to form a beta-anomeric nucleoside in high yield.
5175268 DNA ENCODING RECOMBINANT HUMAN LYMPHOTOXIN
5175266 NUCLEOSIDES AND OLIGONUCLEOSIDES WITH A PHOSPHATE-FREE INTERNUCLEOSIDE BACKBONE AND PROCESS FOR PREPARING THE SAME Rajender S Varma, Michael E Hogan, Ganapathi R Revankar, Takkellapati Rao assigned to Triplex Pharmaceutical Corporation; Baylor College of Medici Nucleoside derivatives which contain a nucleobase, a sugar and an amino acid backbone of the structure: See Patent for Chemical Structure where R’ refers to the various amino acid side chains or their blocked equivalent and R refers to a nucleo-base or its blocked equivalent. The synthesis of these nucleoside derivatives proceeds by a series of steps including oxidation of the 3’-azido nucleoside derivative, coupling to a benzylated ester of an amino acid to yield the amide and hydrogenation. The adenine, guanine, cytosine and thymine nucleosides with an amino acid at the 5’ terminus are synthesized. From such monomers oligonucleotides can be synthesized which possess an amino acid backbone, using either solid state phase chemistry or liquid phase chemistry.
Fujii, Ryuji Susumu Iwasa, Tomoko Marumoto, Reich Igarashi, Tsuzuki, Japan assigned to Takeda Chemical Industries Ltd Lymphotoxin (LT) mutein (genetically-altered LT) is disclosed that has the following amino acid sequence, or a portion of an active portion of said protein, where 10 to 2 1 amino acids of LT being deleted from N-terminus and which has Pro or Phe at the N-terminus: See Patent for Chemical Structure Ala-His-Leu-Ile-Gly AspPro-Ser-Lys- Gln-Asn-Ser-Leu-Leu Trp-ArgAla-Asn- Thr-Asp-Arg-Ala-Phe-Leu Gln-AspGly- Phe-Ser-Leu-Ser Asn-Asn-Ser-Leu-LeuVal-Pro-Thr-Ser-Gly Ile-Tyr-Phe-Val- Tyr-SerGln-Val Val-Phe-Ser-Gly-Lys- Ala-Tyr-Ser-Pro Pro-Leu-Tyr-Leu-Ala Lys-Ala-Thr-Ser-SerHis-Glu-Val-GlnLeu-Phe-Ser-Ser-Gln TyrPro-Phe-HisVal-Pro-Leu-Leu Ser-Ser-GlnLys-Met- Val-Tyr-Pro-Gly-Leu Gln-Glu-ProTrp- Leu-His-Ser-Met-Tyr His-Gly-Ala-AlaPhe-Gln-Leu-Thr Gln-Gly-Asp-Gln-LeuSerThr-His-Thr-Asp Gly-Ile-Pro-HisLeu-ValLeu-Ser-Pro Ser-Thr-Val-PhePhe-Gly-AlaPhe-Ala-Leu-OH Wherein Rl is Pro or Phe, R2 is a peptide chain represented by the following sequence: See Patentfor Tabular presentation PS or a portion thereof and n is 0 or 1. The LT mutein can be recovered in a higher yield and purified more efficiently under mild conditiom which does not harm the LT’s biological activity, than the whole LT.
for DNA sequencing and as hybridization probes, linkers and adapters in the cloning of genes.
5175252 CLONED GENE ENCODING FOR BACTERIOCIN FROM PEDIOCOCCUS ACIDILACTICI John D Marugg, Adrianus M Ledeboer, Peter A Vandenbergh, James Henderson, Utrecht, FL, Netherlands assigned to Quest International Flavors & Food Ingredients Co Isolation and identification of a gene encoding for a bacteriocin precursor in Pediococcus acidilactici, cloning of the gene in a vector plasmid and transformation to bacteria is described. The bacteriocin is particularly useful for inhibiting Listeria in food products.
ix
5175267 STEREOSELECTIVE GLYCOSYLATION OF HETERCYCLIC BASES Chung K Chu assigned to University of Georgia Research Foundation Inc A method of preparation of 2’,3’-dideoxy and 2’,3’-dideoxy-2, 3’-didehydronucleosides that includes the step of condensing a l-O-activated2-(aromatic or aliphatic)-selenenyl-5-0 protected ribose with a protected heterocyclic base in the presence of trimethybilyl triflate or a Lewis acid to form a beta-anomeric nucleoside in high yield.
5175268 DNA ENCODING RECOMBINANT HUMAN LYMPHOTOXIN
5175266 NUCLEOSIDES AND OLIGONUCLEOSIDES WITH A PHOSPHATE-FREE INTERNUCLEOSIDE BACKBONE AND PROCESS FOR PREPARING THE SAME Rajender S Varma, Michael E Hogan, Ganapathi R Revankar, Takkellapati Rao assigned to Triplex Pharmaceutical Corporation; Baylor College of Medici Nucleoside derivatives which contain a nucleobase, a sugar and an amino acid backbone of the structure: See Patent for Chemical Structure where R’ refers to the various amino acid side chains or their blocked equivalent and R refers to a nucleo-base or its blocked equivalent. The synthesis of these nucleoside derivatives proceeds by a series of steps including oxidation of the 3’-azido nucleoside derivative, coupling to a benzylated ester of an amino acid to yield the amide and hydrogenation. The adenine, guanine, cytosine and thymine nucleosides with an amino acid at the 5’ terminus are synthesized. From such monomers oligonucleotides can be synthesized which possess an amino acid backbone, using either solid state phase chemistry or liquid phase chemistry.
Fujii, Ryuji Susumu Iwasa, Tomoko Marumoto, Reich Igarashi, Tsuzuki, Japan assigned to Takeda Chemical Industries Ltd Lymphotoxin (LT) mutein (genetically-altered LT) is disclosed that has the following amino acid sequence, or a portion of an active portion of said protein, where 10 to 2 1 amino acids of LT being deleted from N-terminus and which has Pro or Phe at the N-terminus: See Patent for Chemical Structure Ala-His-Leu-Ile-Gly AspPro-Ser-Lys- Gln-Asn-Ser-Leu-Leu Trp-ArgAla-Asn- Thr-Asp-Arg-Ala-Phe-Leu Gln-AspGly- Phe-Ser-Leu-Ser Asn-Asn-Ser-Leu-LeuVal-Pro-Thr-Ser-Gly Ile-Tyr-Phe-Val- Tyr-SerGln-Val Val-Phe-Ser-Gly-Lys- Ala-Tyr-Ser-Pro Pro-Leu-Tyr-Leu-Ala Lys-Ala-Thr-Ser-SerHis-Glu-Val-GlnLeu-Phe-Ser-Ser-Gln TyrPro-Phe-HisVal-Pro-Leu-Leu Ser-Ser-GlnLys-Met- Val-Tyr-Pro-Gly-Leu Gln-Glu-ProTrp- Leu-His-Ser-Met-Tyr His-Gly-Ala-AlaPhe-Gln-Leu-Thr Gln-Gly-Asp-Gln-LeuSerThr-His-Thr-Asp Gly-Ile-Pro-HisLeu-ValLeu-Ser-Pro Ser-Thr-Val-PhePhe-Gly-AlaPhe-Ala-Leu-OH Wherein Rl is Pro or Phe, R2 is a peptide chain represented by the following sequence: See Patentfor Tabular presentation PS or a portion thereof and n is 0 or 1. The LT mutein can be recovered in a higher yield and purified more efficiently under mild conditiom which does not harm the LT’s biological activity, than the whole LT.