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5352600 Purified thermostable enzyme
266
PATENT ABSTRACTS thermostability: stable below 30 degrees C., and e) inhibition: by Cu2 +- ions.
5352596 PSEUDORABIES VIRUS DELETION MUTANTS INVOLVING THE EPO AND LLT GENES Andrew Cbeung, Ronald Wesley assigned to The United States of America as represented by the Secretary of Agriculture An attenuated pseudorabies virus (PRV) having a reduced ability to reactivate from latency is produced by introducing (1) a genomic modification in the early protein 0 (EP0) gene whereby said virus is characterized by the inability to express the early protein 0; or (2) a genomic modification in t h e large latency transcript (LLT) gene whereby said virus is characterized by disruption of the synthesis of said large latency transcript; or (3) the genomic modifications described in both (1) and (2). The attenuated virus is useful in a vaccine for psnedorabies-susceptible 8nimals, particularly swine. Swine vaccinated with a deletion mutant in the EP0/LLT overlap region displayed reduced virus shedding and fewer clinical signs than animals inoculated with a wild type virus. The deletion mutant-vaccinated swine also harbored less PRV DNA in the nervous tissue and showed reduced ability to reactivate the virus.
PURIFIED
THERMOSTABLE ENZYME
David Gelfand, Susann Stoffei assigned to Hoffmann-La Roche Inc A purified thermostable enzyme is obtained that has unique characteristics. Preferably the enzyme is isolated from the Thermus aqnaticus species and has a molecular weight o f about 86,000-95,000 daltons. The thermostable enzyme may be native or recombinant and may be used in a temperature-cycling chain reaction wherein at least one nucleic acid eSeClxffence is amplified in quantity from an ring sequence with the aid of selected primers and nucleotide triphosphates. The enzyme is preferably stored in a buffer containing non-ionic detergents that lends stability to the enzyme.
5352603 HIGHLY ALKALINE PROTEASES
5352599 CO-ENZYME-INDEPENDENT
5352600
L-
SORBOSONE DEHYDROGENASE OF GLUCONOBACTER OXYDANS: ISOLATION, CHARACTERIZATION, AND CLONING AND AUTOLOGUS EXPRESSION OF THE GENE Akiko Fujiwara, Tatsuo Hoshino, Masako Shinjoh, gAmakura, Japan assigned to Hoffmann-La Roche Inc A novel cnenzyme independent L-sorbosone dehydrogenase originating from a microoreani~m belonging to the genus Gluconobactcr ~xydans which acts on L-sorbosone to produce 2-keto-L-gulonic acid. The enzyme has the following physico-chemical properties: a) optimum pH: about 7.0, b) optnnum temperatree: about 30 degrees C. to about 40 degrees C., c) molecular sturucture: consisting of one type of unit having a molecular w~e~t of about 47,500+/-5,000 as measured by sodium dodecyl sulfate polyacrylamide gel electrophoresis, d)
Roman Vetter, Detlef Wilke, Antoine Amory, Andre Schomburg Diet.mar Clippe, Wolfgang Aehle, Burgdorf, Federal Republic Of Germany assigned to Kali-Chemie AG; Gesellschaft fuer Biotechnologische Forschung m Novel, optimized highly alkaline proteases which are suitable for use in detergent formulations are prepared by employing microorganisms transformed by mutated DNA sequences. The mutated sequences are obtained starting from DNA sequences which code for hi~ldy alkaline protease usually produced by Bacillus e~fineS by altering these DNA sequences in ed positions by directed mutagenesis (point mutation) in such a way that the codon in which the .point mutation is located now codes for an anuno acid which is more strongly basic than the original amino acid. The result is highly alkaline prot__~J~a~_.sin which oriBinal amino acids have been replaced by more strongly basic amino acids, preferably by the amino acids lysine or arsinine. Synthetic oligonucleotides, DNA sequences, vectors and transformed microorganisms which are used for generating and obtaining the optimized highly alkaline protease are also described.
PATENT ABSTRACTS thermostability: stable below 30 degrees C., and e) inhibition: by Cu2 +- ions.
5352596 PSEUDORABIES VIRUS DELETION MUTANTS INVOLVING THE EPO AND LLT GENES Andrew Cbeung, Ronald Wesley assigned to The United States of America as represented by the Secretary of Agriculture An attenuated pseudorabies virus (PRV) having a reduced ability to reactivate from latency is produced by introducing (1) a genomic modification in the early protein 0 (EP0) gene whereby said virus is characterized by the inability to express the early protein 0; or (2) a genomic modification in t h e large latency transcript (LLT) gene whereby said virus is characterized by disruption of the synthesis of said large latency transcript; or (3) the genomic modifications described in both (1) and (2). The attenuated virus is useful in a vaccine for psnedorabies-susceptible 8nimals, particularly swine. Swine vaccinated with a deletion mutant in the EP0/LLT overlap region displayed reduced virus shedding and fewer clinical signs than animals inoculated with a wild type virus. The deletion mutant-vaccinated swine also harbored less PRV DNA in the nervous tissue and showed reduced ability to reactivate the virus.
PURIFIED
THERMOSTABLE ENZYME
David Gelfand, Susann Stoffei assigned to Hoffmann-La Roche Inc A purified thermostable enzyme is obtained that has unique characteristics. Preferably the enzyme is isolated from the Thermus aqnaticus species and has a molecular weight o f about 86,000-95,000 daltons. The thermostable enzyme may be native or recombinant and may be used in a temperature-cycling chain reaction wherein at least one nucleic acid eSeClxffence is amplified in quantity from an ring sequence with the aid of selected primers and nucleotide triphosphates. The enzyme is preferably stored in a buffer containing non-ionic detergents that lends stability to the enzyme.
5352603 HIGHLY ALKALINE PROTEASES
5352599 CO-ENZYME-INDEPENDENT
5352600
L-
SORBOSONE DEHYDROGENASE OF GLUCONOBACTER OXYDANS: ISOLATION, CHARACTERIZATION, AND CLONING AND AUTOLOGUS EXPRESSION OF THE GENE Akiko Fujiwara, Tatsuo Hoshino, Masako Shinjoh, gAmakura, Japan assigned to Hoffmann-La Roche Inc A novel cnenzyme independent L-sorbosone dehydrogenase originating from a microoreani~m belonging to the genus Gluconobactcr ~xydans which acts on L-sorbosone to produce 2-keto-L-gulonic acid. The enzyme has the following physico-chemical properties: a) optimum pH: about 7.0, b) optnnum temperatree: about 30 degrees C. to about 40 degrees C., c) molecular sturucture: consisting of one type of unit having a molecular w~e~t of about 47,500+/-5,000 as measured by sodium dodecyl sulfate polyacrylamide gel electrophoresis, d)
Roman Vetter, Detlef Wilke, Antoine Amory, Andre Schomburg Diet.mar Clippe, Wolfgang Aehle, Burgdorf, Federal Republic Of Germany assigned to Kali-Chemie AG; Gesellschaft fuer Biotechnologische Forschung m Novel, optimized highly alkaline proteases which are suitable for use in detergent formulations are prepared by employing microorganisms transformed by mutated DNA sequences. The mutated sequences are obtained starting from DNA sequences which code for hi~ldy alkaline protease usually produced by Bacillus e~fineS by altering these DNA sequences in ed positions by directed mutagenesis (point mutation) in such a way that the codon in which the .point mutation is located now codes for an anuno acid which is more strongly basic than the original amino acid. The result is highly alkaline prot__~J~a~_.sin which oriBinal amino acids have been replaced by more strongly basic amino acids, preferably by the amino acids lysine or arsinine. Synthetic oligonucleotides, DNA sequences, vectors and transformed microorganisms which are used for generating and obtaining the optimized highly alkaline protease are also described.