8605802 Reactor for cultivating biological material such as immobilised cells

8605802 Reactor for cultivating biological material such as immobilised cells

PATENT ABSTRACTS 171 8605802 8606279 REACTOR FOR CULTIVATING BIOLOGICAL MATERIAL SUCH AS IMMOBILISED CELLS MODULATING ENDOTOXIC ACTIVITY OF ACUT...

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PATENT ABSTRACTS

171

8605802

8606279

REACTOR FOR CULTIVATING BIOLOGICAL MATERIAL SUCH AS IMMOBILISED CELLS

MODULATING ENDOTOXIC ACTIVITY OF

ACUTE PHASE PROTEIN LIPOPOLYSACCHARIDES,

Graham Arthur DAVIES, Ferda MAVITUNA, Wychwood, Sand Lane, Nether AIderley, Macclesfield, Cheshire SKI0 4TS, United Kingdom assigned to NATIONAL RESEARCH DEVELOPMENT CORPORATION A reactor (10) for cultivating biological material is colonised with plant cells (3) in channels (2a) of a support matrix. The biological material cannot pass out of the channels. Each colonised channel adjoins several non-colonised channels (2), viz. a nutrient supply channel, an extractant channel, a heat-transfer channel and a gas supply channel. The walls separating the different pairs of these channels are permeable to the relevant material only.

COMPOSITIONS

AND METHODS

Richard J ULEV1TCH, Peter S TOBIAS assigned to SCRIPPS CLINIC AND RESEARCH FOUNDATION A therapeutic glycoprotein-containing composition for treating an animal host, methods, polypeptides and antibodies related to that glycoprotein. The composition contains an effective amount of a glycoprotein that: (a) is present in acute phase serum, but is substantially absent from normal serum; (b) binds to gramnegative bacterially secreted lipopolysaccharide in vitro in the serum of the animal treated; and (c) retards in vitro binding of the lipopolysaccharide to high density lipoprotein present in the normal serum of the animal host.

8605814 A SOLUBILIZABLE, FIBRIN BASED COMPOSITION AND ITS USE, IN DETERMINATIONS OF FIBRINOLYSIS PARAMETERS Mats Gustaf RA@oNBY, BioPool AB, Box 4025, S-900 04 Umea@o, Sweden assigned to BIOPOOL AB A fully solubilizable fibrin based composition, which is characterized by the combination that the fibrin is desAA-fibrin or desAA-fibrin from which the C-terminal portions of the alphachains have been removed by enzymatic digestion, and that the solubilizing agent is a tetrapeptide containing the amino acid sequence -L-prolyI-L-arginyl-. preferably glycyI-L-prolylL-arginyI-L-prolin. The full solubility of the fibrin makes possible new uses within the area of determination of important fibrinolytical parameters, and the invention also relates to three such important alternative uses. A first use according to the invention is the use of the composition in connection with detection or quantification of the activity of the enzyme tissue plasminogen activator. A first alternative use means that the composition is used for the detection of soluble fibrin in biological fluids, and a second alternative use means that the composition is used for measuring or studying fibrinolytic activity in vitro or in vivo through the addition of the composition and registration of the degradation of the fibrin.

8606298 METHOD AND APPARATUS FOR AUTOMATED SYNTHESIS OF PEPTIDES Marcus J HORN. William K MILLER assigned to APPLIED PROTEIN TECHNOLOGIES INC, A system for the automated synthesis of peptides includes a reaction vessel (12) that has a single port (12a) for both injection and withdrawal of the various fluids used in the peptide synthesis sequence, a plurality of amino acid reservoirs (14a -14n) and a plurality of solvent and reagent reservoirs ( 16a - 16n) for the synthesis of the peptide chains. A volume displacement pump regulates the pressure within the vessel (12) and in combination with valves (44, 48, 72, 66, 82 and 92) allows connection of a selected reservoir (14a, 16a) to the reaction vessel (12). Maintaining the system at a reference pressure enables transfer of amino acids, reagents and solvents from the reservoirs ( 14a. 16a) to the reaction vessel 02) without using high vacuum conditions. The system is also optionally equipped with a yield monitor (120) that assesses the completeness of each amino acid addition.