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4965194 Pyruvate oxidase and an analytical method using the same
PATENT ABSTRACTS ove, chlorine bleach, and at least one additional detergent component.
4965188 PROCESS FOR AMPLIFYING, DETECTING, AND/OR CLONING NUCLEIC ACID SEQUENCES USING A THERMOSTABLE ENZYME Kary Mullis, Henry A Erlich, David Gelfand, Glenn Horn, Randall Saiki assigned to Cetus Corporation A process for amplifying any target nucleic acid sequence contained in a nucleic acid or mixture thereof comprises treating separate complementary strands of the nucleic acid with a molar excess of two oligonucleotide primers and extending the primers with a thermostable enzyme to form complementary primer extension products which act as templates for synthesizing the desired nucleic acid sequence. The amplified sequence can be readily detected. The steps of the reaction can be repeated as often as desired and involve temperature cycling to effect hybridization, promotion of activity of the enzyme, and denaturation of the hybrids formed.
4~51~ DETECTION OF MICROBIAL BETA-LACTAMASE Kirk C S Chen assigned to Washington Research Foundation An improved developer for a method for the specific detection of the presence of betalactamase from microbial sources is disclosed. The method utilizes a beta-lactam ringcontaining substrate whose amide bond is hydrolyzed in the presence of beta-lactamase. A substrate which includes a beta-lactam antibiotic with an acyl side chain containing an alphaamino group and an alpha-phenyl group or its derivatives is first contacted with an organism thought to produce beta-lactamase or a cell-free beta-lactamase preparation, and, subsequently, it is determined whether the reaction product between the unhydrolyzed substrate, the end products and the organism or the preparation fluoresces. Fluorescence is the indication of beta-lactamase activity. The developer comprises the addition of an oxidizing agent (preferably also containing formaldehyde) to the
105
reaction product to enhance the fluorescence. The oxidizing agent is selected from the group consisting of A g + , H g + + , H202, 13-, 104-, persulfate, Pd + + , p-hydroxymercuribenzoate, and mixtures thereof.
4~51~ PYRUVATE OXIDASE AND AN ANALYTICAL METHOD USING THE SAME Kazumi Yamamoto, Toshiro Kikuchi, Shigenori Emi, Tsuruga, Japan assigned to Toyo Boseki Kabushiki Kaisha A pyruvate oxidase with excellent thermal stability, which is stable at pH 7.0 for 10 minutes at a temperature of up to 45 degrees C., an analytical method using said pyruvate oxidase, and an analytical reagent used for said method•
4968605 IMMOBILIZATION OF ENZYMES ON POROUS MELT SPUN POLYAMIDE YARNS Nigel Hayman, Cheltenham, United Kingdom assigned to Imperial Chemical Industries plc An immobilized enzyme structure in which molecules of one or more enzymes are attached to chemically active groups located on surface in the structure, such structure being composed of melt spun polyamide fibres comprising spaced fibrils of polyamide which are substantially aligned to the axis of the fibre, such aligned spaced fibrils being interconnected to each other in a random manner.
4970145 IMMOBILIZED ENZYME ELECTRODES Hugh P Bennetto, Gerard M Delaney, Jeremy Mason, Christopher Thurston, John L Stifling, David R DeKeyzer, London, United Kingdom assigned to Cambridge Life Sciences plc Enzyme electrodes are disclosed which are capable of responding amperometrically to the catalytic activity oftbe enzyme in the presence of its respective substrate and comprising the en-
4965188 PROCESS FOR AMPLIFYING, DETECTING, AND/OR CLONING NUCLEIC ACID SEQUENCES USING A THERMOSTABLE ENZYME Kary Mullis, Henry A Erlich, David Gelfand, Glenn Horn, Randall Saiki assigned to Cetus Corporation A process for amplifying any target nucleic acid sequence contained in a nucleic acid or mixture thereof comprises treating separate complementary strands of the nucleic acid with a molar excess of two oligonucleotide primers and extending the primers with a thermostable enzyme to form complementary primer extension products which act as templates for synthesizing the desired nucleic acid sequence. The amplified sequence can be readily detected. The steps of the reaction can be repeated as often as desired and involve temperature cycling to effect hybridization, promotion of activity of the enzyme, and denaturation of the hybrids formed.
4~51~ DETECTION OF MICROBIAL BETA-LACTAMASE Kirk C S Chen assigned to Washington Research Foundation An improved developer for a method for the specific detection of the presence of betalactamase from microbial sources is disclosed. The method utilizes a beta-lactam ringcontaining substrate whose amide bond is hydrolyzed in the presence of beta-lactamase. A substrate which includes a beta-lactam antibiotic with an acyl side chain containing an alphaamino group and an alpha-phenyl group or its derivatives is first contacted with an organism thought to produce beta-lactamase or a cell-free beta-lactamase preparation, and, subsequently, it is determined whether the reaction product between the unhydrolyzed substrate, the end products and the organism or the preparation fluoresces. Fluorescence is the indication of beta-lactamase activity. The developer comprises the addition of an oxidizing agent (preferably also containing formaldehyde) to the
105
reaction product to enhance the fluorescence. The oxidizing agent is selected from the group consisting of A g + , H g + + , H202, 13-, 104-, persulfate, Pd + + , p-hydroxymercuribenzoate, and mixtures thereof.
4~51~ PYRUVATE OXIDASE AND AN ANALYTICAL METHOD USING THE SAME Kazumi Yamamoto, Toshiro Kikuchi, Shigenori Emi, Tsuruga, Japan assigned to Toyo Boseki Kabushiki Kaisha A pyruvate oxidase with excellent thermal stability, which is stable at pH 7.0 for 10 minutes at a temperature of up to 45 degrees C., an analytical method using said pyruvate oxidase, and an analytical reagent used for said method•
4968605 IMMOBILIZATION OF ENZYMES ON POROUS MELT SPUN POLYAMIDE YARNS Nigel Hayman, Cheltenham, United Kingdom assigned to Imperial Chemical Industries plc An immobilized enzyme structure in which molecules of one or more enzymes are attached to chemically active groups located on surface in the structure, such structure being composed of melt spun polyamide fibres comprising spaced fibrils of polyamide which are substantially aligned to the axis of the fibre, such aligned spaced fibrils being interconnected to each other in a random manner.
4970145 IMMOBILIZED ENZYME ELECTRODES Hugh P Bennetto, Gerard M Delaney, Jeremy Mason, Christopher Thurston, John L Stifling, David R DeKeyzer, London, United Kingdom assigned to Cambridge Life Sciences plc Enzyme electrodes are disclosed which are capable of responding amperometrically to the catalytic activity oftbe enzyme in the presence of its respective substrate and comprising the en-