Abstract: The present invention relates to a novel composition with milk of immunized camelid, particularly, (Camelus dromedarius) as the main component (i.e. active ingredient) and a method for the treatment or prevention of gastrointestinal infections, particularly, infections caused by Escherichia coli (E. coli), Helicobacter Pylori (H. pylori), Campylobacter jejuni (C. jejuni), Salmonella enterica, Shigella dysenteriae, Clostridium perfringens, or Yersinia enterocolitica. Said composition is prepared in the form of pharmaceutical, nutraceutical, or health food preparations. The present invention also discloses a process of preparing said composition.

Abstract: The present invention relates to a novel pharmaceutical composition with milk of immunized camelid, particularly Camelus dromedaries as the main component (i.e. active ingredient) and a method for the treatment or prevention of skin or mucus membrane infections, particularly Acne vulgaris. The present invention also discloses a process of preparing said composition.

Abstract: The present invention relates to a novel pharmaceutical composition with milk of immunized camelid, particularly Camelus dromedarius as the main component (i.e. active ingredient) and a method for the treatment or prevention of skin or mucus membrane infections, particularly Acne vulgaris. The present invention also discloses a process of preparing said composition.

Abstract: The present invention relates to a specific phenylboronic acid compound having anti-cancer, anti-inflammatory, and anti-microbial activity, in addition to a pharmaceutical composition comprising the same. The present invention also discloses a process for preparing said compound.

Abstract: An isolated recombinant luciferase having luciferase activity. The recombinant luciferase has an amino acid sequence which differs from the wild-type luciferase from Phtotinus pyralis, Luciola mingrelica, Luciola cruciata, Luciola lateralis, Hotaria parvula, Pyrophorus plagiophthalamus, Lampyris noctiluca, Pyrocoelia miyako or Photinus pennsylvanica. In the seguence of the recombinant luciferase, the amino acid residue corresponding to phenylalanine 295 in Photinus pyralis wild-type luciferase or to leucine 297 in Luciola mingrelica, Luciola cruciata or Luciola lateralis wild-type luciferases, is mutated compared to the corresponding amino acid which appears in the corresponding wild-type luciferase sequence. The recombinant luciferase has increased thermostability compared to the corresponding wild-type luciferase.

Abstract: An isolated recombinant luciferase having luciferase activity. The recombinant luciferase has an amino acid sequence which differs from the wild-type luciferase from Photinus pyralis, Luciola mingrelica, Luciola cruciata, Luciola lateralis, Hotaria parvula, Pyrophorus plagiophthalamus, Lampyris noctiluca, Pyrocoelia miyako or Photinus pennsylvanica. In the sequence of the recombinant luciferase, the amino acid residue corresponding to phenylalanine 295 in Photinus pyralis wild-type luciferase or to leucine 297 in Luciola mingrelica, Luciola cruciata or Luciola lateralis wild-type luciferases, is mutated compared to the corresponding amino acid which appears in the corresponding wild-type luciferase sequence. The recombinant luciferase has increased thermostability compared to the corresponding wild-type luciferase.

Abstract: A sensing system comprises a material having a matrix structure in which a plurality of sensing elements are embedded, the sensing elements having electron distribution and/or transport properties that change in response to a change in a physical or chemical property of the material. The sensing system further comprises a receiver, including an antenna, the receiver arranged to receive a source RF signal and a returned RF signal, the returned RF signal being received from the material. A change in the electron distribution and/or transport properties of the sensing elements cause the source RF signal to change, such that a change in a property of the material can be determined from the returned RF signal. A corresponding method of sensing a change in a property of a material is also provided.

Abstract: The present invention relates to a novel composition with milk of immunized camelid, particularly, (Camelus dromedarius) as the main component (i.e. active ingredient) and a method for the treatment or prevention of gastrointestinal infections, particularly, infections caused by Escherichia coli (E. coli), Helicobacter Pylori (H. pylori), Campylobacter jejuni (C. jejuni), Salmonella enterica, Shigella dysenteriae, Clostridium perfringens, or Yersinia enterocolitica. Said composition is prepared in the form of pharmaceutical, nutraceutical, or health food preparations. The present invention also discloses a process of preparing said composition.

Abstract: The present invention relates to a novel pharmaceutical composition with milk of immunized camelid, particularly Camelus dromedarius as the main component (i.e. active ingredient) and a method for the treatment or prevention of skin or mucus membrane infections, particularly Acne vulgaris. The present invention also discloses a process of preparing said composition.

Abstract: The present invention relates to a specific phenylboronic acid compound having anti-cancer, anti-inflammatory, and anti-microbial activity, in addition to a pharmaceutical composition comprising the same. The present invention also discloses a process for preparing said compound.

Abstract: An isolated recombinant luciferase having luciferase activity. The recombinant luciferase has an amino acid sequence which differs from the wild-type luciferase from Photinus pyralis, Luciola mingrelica, Luciola cruciata, Luciola lateralis, Hotaria parvula, Pyrophorus plagiophthalamus, Lampyris noctiluca, Pyrocoelia miyako or Photinus pennsylvanica. In the sequence of the recombinant luciferase, the amino acid residue corresponding to phenylalanine 295 in Photinus pyralis wild-type luciferase or to leucine 297 in Luciola mingrelica, Luciola cruciata or Luciola lateralis wild-type luciferases, is mutated compared to the corresponding amino acid which appears in the corresponding wild-type luciferase sequence. The recombinant luciferase has increased thermostability compared to the corresponding wild-type luciferase.

Abstract: A sensing system comprises a material having a matrix structure in which a plurality of sensing elements are embedded, the sensing elements having electron distribution and/or transport properties that change in response to a change in a physical or chemical property of the material. The sensing system further comprises a receiver, including an antenna, the receiver arranged to receive a source RF signal and a returned RF signal, the returned RF signal being received from the material. A change in the electron distribution and/or transport properties of the sensing elements cause the source RF signal to change, such that a change in a property of the material can be determined from the returned RF signal. A corresponding method of sensing a change in a property of a material is also provided.

Abstract: An isolated recombinant luciferase having luciferase activity. The recombinant luciferase has an amino acid sequence which differs from the wild-type luciferase from Photinus pyralis, Luciola mingrelica, Luciola cruciata, Luciola lateralis, Hotaria parvula, Pyrophorus plagiophthalamus, Lampyris noctiluca, Pyrocoelia miyako or Photinus pennsylvanica. In the sequence of the recombinant luciferase, the amino acid residue corresponding to phenylalanine 295 in Photinus pyralis wild-type luciferase or to leucine 297 in Luciola mingrelica, Luciola cruciata or Luciola lateralis wild-type luciferases, is mutated compared to the corresponding amino acid which appears in the corresponding wild-type luciferase sequence. The recombinant luciferase has increased thermostability compared to the corresponding wild-type luciferase.

Abstract: A protein having luciferase activity and at least 60% similarity to luciferase from Photinus pyralis, Luciola mingrelica, Luciola cruciata or Luciola lateralis.

Abstract: Proteins are provided having luciferase activity with lower Km than wild-type luciferases by altering the amino acid residue at position 270 of the wild-type to an amino acid other than glutamate. Greater heat stability than wild-type luciferases while retaining the lower Km is provided by also replacing the glutamate equivalent to that at position 354 of Photinus pyralis luciferase or 356 of Luciola luciferases with an alternative amino acid, particularly lysine and/or the amino acid residue at 215 of Photinus pyralis and 217 of the Luciola species with a hydrophobic amino acid. DNA, vectors and cells that encode for and express the proteins are also provided as are test kits and reagents for carrying out luminescence assays using the proteins of the invention.

Abstract: A biosensor for detecting metal ions of elements such as Hg, Cr, As, Tc, Cu, Ag, Se, V, Mo and U which are capable of being reduced to metal by a reductase enzyme. The reductase enzyme is contained in an immobilized enzyme composition also including a cofactor and a coenzyme. The cofactor, for example NADPH, is oxidized by a reaction coupled with the reductase reduction of the metal ions and the cofactor in its oxidized state, e.g., NADP.sup.+, is re-reduced thereby maintaining a supply of the reduced state cofactor by action of the coenzyme in a further oxidation reaction coupled with the cofactor reduction. The further oxidation reaction may be oxidation of an alcohol to an aldehyde brought about by a dehydrogenase coenzyme. The oxidation brought about by the coenzyme, i.e., the amount of oxidized product, is a measure of the amount of oxidized state cofactor produced which, in turn, is a measure of the concentration of metal ions being detected.

Abstract: A cocaine esterase has been isolated from a strain of the bacteria Pseudomonas maltophilta, The cocaine esterase catalyses the debenzoylation of cocaine, This reaction may be used in the detection of cocaine. The enzyme may be incorporated into sensors for this purpose. The cocaine esterase is preferably obtainable from Pseudomonas sp. NCIMB 40427. It catalyzes the debenzoylation of cocaine, has a molecular weight in the unaggregated form of about 120,000 daltons as determined by gel filtration, has esterase activity specifically at the benzoate ester linkage of cocaine, separates at a major band of Rf about 0.2 on PAGE in its aggregated form, and it is completely inhibited by 1 mM phenylmethylsulphonyl fluoride but ineffectively inhibited by 1 mM eserine, each determined at 30.degree. C. with respect to 2 mM cocaine as substrate.

Abstract: Two enzymes, one an acetylmorphine carboxyesterase (AMCE), the other a morphine dehydrogenase (MDH), have been isolated from bacteria. The AMCE degrades heroin to morphine and the MDH oxidizes morphine to morphinone, with the aid of a cofactor. More particularly, the invention pertains to a process for preparing a 6-ketone from morphine or a methyl or ethyl derivative thereof. The process comprises oxidizing morphine or an ether derivative in the presence of a morphine dehydrogenase and the cofactor NADP.sup.+. These reactions are used in detection of heroin (using the two reactions coupled together) or morphine. The enzymes can be incorporated in sensors for this purpose.

Abstract: A separation medium for use in protein separation comprising a water-insoluble matrix carrying a plurality of polyamine groupings, the polyamine groupings having at least three basic nitrogen atoms, the basic nitrogen atoms being separated from each other by a chain of at least two intervening carbon atoms, there being a total of 5 such intervening carbon atoms when there is a total of three nitrogen atoms in each polyamine group, which may be used for at least partially purifying factor VIII.

Abstract: Two enzymes, one an acetylmorphine carboxyesterase (AMCE), the other a morphine dehydrogenase (MDH), have been isolated from bacteria. The AMCE degrades heroin to morphine and the MDH oxidises morphine to morphinone, with the aid of a cofactor. These reactions are used in detection of heroin (using the two reactions coupled together) or morphine. The enzymes can be incorporated in sensors for this purpose.