Abstract: Transgenic non-human animals that express the ?3 subunit of PRKAG are described, as well as methods of using the transgenic non-human animals as models for improving treatment, prevention, or diagnosis of diseases related to energy metabolism, including obesity, dyslipidemia, insulin resistance syndrome, and type 2 diabetes.

Abstract: The present invention relates to a polypeptide which is flavin-containing monooxygenase 3 (FMO3), wherein said FMO3 is a polypeptide comprising at least a sequence having at least 85% identity with the polypeptide sequence SEQ ID NO: 15, in particular to a polypeptide which is a functionally altered mutant of flavin-containing mono oxygenase 3 (FMO3) leading to a buildup of trimethylamine in an animal. Further, the invention relates to nucleic acid sequences encoding said polypeptide, and to the complements of such nucleic acid sequences. Such nucleic acid sequences and fragments thereof may be useful e.g. as primers. The invention further relates to various methods for determining the presence in e.g. a nucleic acid sample of a nucleic acid sequence encoding a mutated FMO3 polypeptide.

Abstract: Transgenic non-human animals that express the ?3 subunit of PRKAG are described, as well as methods of using the transgenic non-human animals as models for improving treatment, prevention, or diagnosis of diseases related to energy metabolism, including obesity, dyslipidemia, insulin resistance syndrome, and type 2 diabetes.

Abstract: The present invention relates to a polypeptide which is a flavin-containing monooxygenase 3 (FMO3), wherein said FMO3 is a polypeptide comprising at least a sequence having at least 85% identity with the polypeptide sequence SEQ ID NO: 15, in particular to a polypeptide which is a functionally altered mutant of flavin-containing mono oxygenase 3 (FMO3) leading to a buildup of trimethylamine in an animal. Further, the invention relates to nucleic acid sequences encoding said polypeptide, and to the complements of such nucleic acid sequences. Such nucleic acid sequences and fragments thereof may be useful e.g. as primers. The invention further relates to various methods for determining the presence in e.g. a nucleic acid sample of a nucleic acid sequence encoding a mutated FMO3 polypeptide.

Abstract: Transgenic non-human animals that express the ?3 subunit of PRKAG are described, as well as methods of using the transgenic non-human animals as models for improving treatment, prevention, or diagnosis of diseases related to energy metabolism, including obesity, dyslipidemia, insulin resistance syndrome, and type 2 diabetes.

Abstract: Disclosed herein are embodiments to screen an animal for the presence or absence of polymorphisms in the following gene: CKM, SCN4?, and LDH?.

Abstract: The present invention relates to a polypeptide which is a flavin-containing monooxygenase 3 (FMO3), wherein said FMO3 is a polypeptide comprising at least a sequence having at least 85% identity with the polypeptide sequence SEQ ID NO: 15, in particular to a polypeptide which is a functionally altered mutant of flavin-containing mono oxygenase 3 (FMO3) leading to a buildup of trimethylamine in an animal. Further, the invention relates to nucleic acid sequences encoding said polypeptide, and to the complements of such nucleic acid sequences. Such nucleic acid sequences and fragments thereof may be useful e.g. as primers. The invention further relates to various methods for determining the presence in e.g. a nucleic acid sample of a nucleic acid sequence encoding a mutated FMO3 polypeptide.

Abstract: Transgenic non-human animals that express the ?3 subunit of PRKAG are described, as well as methods of using the transgenic non-human animals as models for improving treatment, prevention, or diagnosis of diseases related to energy metabolism, including obesity, dyslipidemia, insulin resistance syndrome, and type 2 diabetes.

Abstract: Methods for determining coat color genotypes in pigs are provided. In particular, these methods are based on determining whether a mutation is/is not present at one or more exon/intron splice sites of the KIT gene. Kits for carrying out such methods are also described.

Abstract: Disclosed herein are embodiments to screen an animal for the presence or absence of polymorphisms in the following gene: CKM, SCN4&agr;, and LDH&agr;.

Abstract: PRKAG3 nucleotide and amino acid sequence variants and methods of detecting such sequence variants are described. Methods for providing risk estimates for development of a metabolic disease also are described and are based on the presence or absence of PRKAG3 sequence variants in a biological sample.

Abstract: PRKAG3 nucleotide and amino acid sequence variants and methods of detecting such sequence variants are described. Methods for providing risk estimates for development of a metabolic disease also are described and are based on the presence or absence of PRKAG3 sequence variants in a biological sample.

Abstract: A superoxide dismutase originally found in extracellular body fluids and therefore termed extracellular superoxide dismutase (EC-SOD) is prepared by growing a cell line, preferably of mammalian origin, producing EC-SOD and recovering the EC-SOD secreted from the cells or by inserting a DNA sequence encoding EC-SOD into a suitable vector, introducing the recombinant vector into a host cell, growing the cell and recovering the EC-SOD produced.EC-SOD may be used for the prophylaxis or treatment of diseases or disorders associated with the presence or formation of superoxide radicals.

Abstract: A superoxide dismutase originally found in extracellular body fluids and therefore termed extracellular superoxide dismutase (EC-SOD) is prepared by growing a cell line, preferably of mammalian origin, producing EC-SOD and recovering the EC-SOD secreted from the cells or by inserting a DNA sequence encoding EC-SOD into a suitable vector, introducing the recombinant vector into a host cell, growing the cell and recovering the EC-SOD produced.EC-SOD may be used for the prophylaxis or treatment of diseases or disorders associated with the presence or formation of superoxide radicals.

Abstract: Extracellular superoxide dismutase (EC-SOD) variants having the superoxide dismutating property of the native EC-SOD and having a modified (reduced or increased) binding to heparin as compared to recombinant EC-SOD C as well as compositions comprising such variants. The EC-SOD variants are polypeptides comprising: 1) amino acids 1-193 of native EC-SOD C and 2) an amino acid sequence which is based on, but different from amino acid moieties 194-222 of recombinant EC-SOD C, either by being truncated or prolonged at the C-terminal end or by having substituted or otherwise modified one or more amino acid moieties of the sequence. Another EC-SOD variant is one which differs from recombinant EC-SOD C by being a glycosylation-free mutant. The variants may be produced by recombinant DNA techniques and are useful in the treatment of various diseases.

Abstract: A superoxide dismutase originally found in extracellular body fluids and therefore termed extracellular superoxide dismutase (EC-SOD) is prepared by growing a cell line, preferably of mammalian origin, producing EC-SOD and recovering the EC-SOD secreted from the cells or by inserting a DNA sequence encoding EC-SOD into a suitable vector, introducing the recombinant vector into a host cell, growing the cell and recovering the EC-SOD produced.EC-SOD may be used for the prophylaxis or treatment of diseases or disorders associated with the presence or formation of superoxide radicals.

Abstract: A superoxide dismutase originally found in extracellular body fluids and therefore termed extracellular superoxide dismutase (EC-SOD) is prepared by growing a cell line, preferably of mammalian origin, producing EC-SOD and recovering the EC-SOD secreted from the cells or by inserting a DNA sequence encoding EC-SOD into a suitable vector, introducing the recombinant vector into a host cell, growing the cell and recovering the EC-SOD produced.EC-SOD may be used for the prophylaxis or treatment of diseases or disorders associated with the presence or formation of superoxide radicals.