Abstract: This invention relates to a novel protease-inhibitor,--which we called GELIN--and to pharmaceutical and cosmetic preparations thereof, containing this compound. GELIN is an inhibitor of human and porcine leucocyte elastase and chymotrypsin. GELIN has specific antibiotic properties. It also relates to the novel use of EGLIN, another chymotrypsin-inhibitor in cosmetic preparations.

Abstract: In a method and apparatus for examining samples comprising individual objects (28) of macromolecular or similar size, or smaller, an instrument element (14) comprises a substrate (16) overlaid with a thin film layer (18) of a material that is electrically conductive and/or at last partly optically opaque. A discontinuity comprising an aperture (26) or an asperity is formed in or on the element (14) in a known location, and the sample (28) is brought to this discontinuity so that it is not necessary to search for the sample by scanning. Energy (e.g. electrical energy or light) is applied to the element (14) and, with the latter and the sample in intimate association, e.g. with the sample inside the aperture (26), changes in the radiation from the sample site resulting from the presence of the sample are detected.

Abstract: A recombinant thermophilic NAD-dependent dehydrogenase having a hydrophobic amino acid at position 104 and/or 102. The enzymes are effective in catalysing the dehydrogenation of homologues of pyruvic acid of formula CnH.sub.2n+1 COCOOH, wherein n is>1, to homologues of lactic acid of formula CH.sub.n H.sub.2n+1 CHOHCOOH, wherein n is>1.

Abstract: A method of providing an electrical circuit wherein a carrier, which is a film of insulating plastic material with a circuit pattern thereon is supported in a mould and a moulding material is applied by the application of heat and pressure to provide a substrate so that the circuit is embedded in or within a three-dimensional surface of the moulded substrate.

Abstract: A method is provided for treating a viral infection in a subject by administering a surfactant and/or a steroid so as to produce a high concentration thereof in the systemic circulation. The method is particularly applicable to the treatment of HIV infections. The use of surfactants and/or steroids in the production of pharmaceutical compositions is described.

Abstract: A method of providing an electrical circuit wherein a carrier, which is a film of insulating plastic material with a circuit pattern thereon is supported in a mould and a moulding material is applied by the application of heat and pressure to provide a substrate so that the circuit is embedded in or within a three-dimensional surface of the moulded substrate.

Abstract: Fibrinolytic enzymes are produced and then isolated from non-cancerous established cell lines, designated as BEB or GPK. These fibrinolytic enzymes differ from those produced by malignant cell lines.

Abstract: A chromatographic packing useful for the separation of oligonucleotides is disclosed. The packing includes an insert porous support particle and a silane bonded phase comprising a weak anion exchange group in close proximity to at least one polar non-ionic group.

Abstract: A plasmid selected from(a) a plasmid conferring resistance to tetracyline (Tc.sup.r) and neomycin (Neo.sup.r) on a host, and being built up by the in vitro ligation of a Neo.sup.r non-chimeric plasmid and a Tc.sup.r non-chimeric plasmid,(b) a deletion, insertion or deletion/insertion derivative of a group (a) plasmid, or(c) a rearrangement derivative of a group (a) or group (b) plasmid are disclosed.The host may be a Bacillus, particularly Bacillus subtilis.

Abstract: Affinity chromatography media are prepared by reacting mono or di-chloro triazine dyes with a solid support matrix containing free hydroxy or amino groups in the presence of an alkali metal hydroxide and an alkali metal salt. In the absence of cyanogen bromide activation, the linkage to the support is entirely via the triazine ring giving high and specific protein-binding capacity. Suitable support matrices include polymers and copolymers of agarose, dextrose, dextran and acrylamide with agarose being particularly preferred. Dye binding levels are much higher than those obtained in the presence of carbonates or bicarbonates.Mono-chlorotriazinyl dyes are bound at a pH which is preferably above 9.5. The reaction time is about 40-60 hours at room temperature, however this may be reduced if the reaction temperature is increased. Dichlorotriazinyl dyes are bound at pH 8 to 12.5 in a few hours at room temperature.

Abstract: A process for the high pressure liquid affinity chromatographic separation of at least one biological or related substance from a mixture in which the contact, washing and eluting phases are performed on a binding material made from a ligand, containing at least one of the groups anthraquinone, phthalocyanine or aromatic azo, coupled to a matrix through a spacer arm, the binding material being so constructed that at least one biological or related substance is retained on the binding material during the contact and washing phases. In one preferred embodiment the ligand is a reactive dye, especially a triazinyl dye, the matrix is agarose or silica and the spacer arm is a substituted aminohexyl group. The chromatographic procedure is preferably performed at 100-3500 psi, at a flow rate of 0.5-2.0 ml/min. The choice of washing and eluting solutions depends on the material to be separated. However buffer solution to wash the column and a desorbing agent to elute the material are preferred.

Abstract: A method for the estimation of an anilide in which the anilide is first hydrolyzed enzymatically to an aniline and then the quantity of the aniline produced is estimated spectrophotometrically preferably colorimetrically.The hydrolysis of the anilide may be catalyzed by any enzyme of the type, EC 3.5.1.13, known as aryl acylamidases. Preferably enzymes isolated from the cells of Pseudomonas fluorescens ATCC 39005 or Pseudomonas putida ATCC 39004 are employed.The aniline may be analyzed, for example, by conversion to an indamine, an indophenol or an indoaniline, followed by colorimetric analysis of the colored quinone-type compound produced. This conversion may take place in the presence of an oxidizing agent, such as a copper (II) salt, and/or a base, such as ammonia.A diagnostic kit to allow the routine use of the above method is also provided.

Abstract: A thermostable glycerokinase enzyme useful in the detection and estimation of glycerol derivatives has a half-life in excess of 1 hour at 55.degree. C. at a protein concentration of less than 2 mg/ml and a pH of 7.8 .+-.0.5 in the absence of any substrate. The enzyme is produced by culturing at least one micro-organism which is capable of growth at a temperature of at least 50.degree. C. in a culture medium in which it will produce said enzyme, disrupting the resulting cells of the micro-organism to release the enzyme and separating the enzyme from the cell debris. The medium normally contains at least 0.1% glycerol but certain strains of micro-organism have been found to be capable of producing thermostable glycerokinase enzyme even in the absence of glycerol. The micro-organism is preferably a Bacillus organism, especially of the stearothermophilus species.

Abstract: Glycerol dehydrogenase enzymes having exeptionally good thermal stability are produced by culturing novel strains of Bacillus stearothermophilus. Procedures for deriving and identifying suitable strains are described. The strains are grown in conventional culture media, preferably containing 0.05 to 4.0%, especially 0.1 to 1.0%, by weight of glycerol or a glycerol analogue at 40.degree.-65.degree. C. and pH 5 to 8. The enzyme is isolated by conventional cell disruption and separation techniques, and typically has a molcular weight of 240,000.+-.30,000, composed of four similar sub-units, and a specific activity of greater than 5 Units per mg protein at 30.degree. C. by the modified assay described. They may be stored as aqueous solutions or a freeze dried solids.The enzymes may be used for assay of serum triglycerides by conventional assay methods, but preferably by the nictotinamide adenine dinucleotide spectrophotometric assay at a pH of 7 to 8.8.