4812392 METHOD AND APPARATUS INCUBATING CELLS
Shinichi Miyake, Shinji Miyasaka, Osaka, Japan assigned to Sumitomo Electric Industries Ltd A method and apparatus for the continued incubation of cells in a liquid culture medium. When the pH value of the culture medium deviates during the incubation from a pH range suited for the growth or multiplication of the cells, the culture medium is automatically replaced. Whether or not the pH value of the culture medium has deviated from the acceptable pH range is determined by measuring the intensity of light absorbed by the culture medium.
4812393 FLUORESCENT DYES AND BIOLOGICAL AND ANALYTICAL USES THEREOF Ramanuj Goswami, Chin H Chen assigned to Eastman Kodak Company Substituted 4-oxo-4H-benz-(d,e) anthracenes are fluorescent dyes which are useful in biomedical studies and analytical determinations. They are particularly useful in assays for living organisms, e.g. microorganisms, carried out at a pH of 9 or less. For these determinations, the fluorescent dyes can be attached to reducible compounds which will release the dye upon reduction. Alternatively, these dyes can be used in assays for hydrolytic enzymes or biological cells containing these enzymes. For these determinations, the dyes are attached to blocking groups.
4812396 METHOD FOR DETECTING ENZYMATIC ACTIVITY USING PARTICLE AGGLUTINATION Robert A Ballas, William A Frey assigned to E I Du Pont De Nemours and Company A method is disclosed for determining enzymatic activity in a liquid sample by particle agglutination or inhibition of particle agglutination.
REAGENT FOR MEASURING AMYLASE ACTIVITY AND MEASURING METHOD THEREOF Hitoshi Kondo, Masao Kageyama, Kyoto, Japan assigned to Unitika Ltd Disclosed is a reagent for measuring amylase activity in body fluids by cleaving an oligosaccharide having a defined chain length with amylase in body fluids to produce a glucose and measuring said glucose, characterized in that the reagent is divided to two portions, the first portion comprises an enzyme for converting a glucose and/or maltose naturally present in body fluids to glucose-6-phosphate, phosphoglucose isomerase, phosphofructokinase and adenosine5'-triphosphate, and the second portion comprises said oligosaccharide being used as a substrate and a phosphoric acid ester of saccharides and/or saccharic acids; and a method for measuring amylase activity in body fluids comprising; eliminating glucose and/or maltose naturally present in body fluids with a first reagent comprising an enzyme for converting the glucose and/or maltose to glucose-6-phosphate, phosphoglucose isomerase, phosphofructokinase and adenosine-5'-triphosphate, adding a second reagent comprising a oligosaccharide substrate and a phosphoric acid ester of saccharides and/or saccharic acids to eliminate the phosphoglucose isomerase activity and to convert the oligosaccharide fragments formed by the action of amylase in body fluids to glucose by means of alpha-glucosidase or maltose phosphorylase, and measuring the amount of the obtained glucose.
4812401 REVERSIBLE AGGLUTINATION MEDIATORS FOR SEPARATING CELLS FROM WHOLE BLOOD Thomas L Tarnowski, Cheng-I Lin, Edwin Ullman assigned to Syntex (U S A ) Inc C o m p o u n d s a n d methods are disclosed for reversibly aggregating particles suspended in a liquid medium. The method comprises combining the liquid medium containing the particles with a polyionic polymer capable of aggregating the particles under conditions suitable for such aggregation. Thereafter, the particles are contacted with a chemical reagent capable of cleaving the
Cleaving Breakthrough: A New Method. Prior to indenting the host and cleaving through the die. The cleaving direction is. Dominated by the crystallographic axis of the thick silicon piece. The indent takes place on the support silicon side (either the front or the back), and the thin-die cleaving will always follow the dominating thick.
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- A self-cleaving element for use in bioseparations has been derived from a naturally occurring, 43 kDa protein splicing element (intein) through a combination of protein engineering and random.