Abstract: This invention describes the new 18-nor steroids (gonatrienes) of general formula (I), in which R1, R2, R3, R6, R7, R8, R9, R11, R11?, R14, R15, R15, R16, R17 and R17? have the meanings that are indicated in the description, as pharmaceutical active ingredients that have in vitro a higher affinity to estrogen receptor preparations of rat prostates than to estrogen receptor preparations of rat uteri and in vivo a preferential action on bone in comparison to the uterus, and/or pronounced action relative to the stimulation of the expression of 5HT2a-receptors and transporters, their production, their therapeutic use and pharmaceutical dispensing forms that contain the new compounds.

Abstract: The invention relates to novel 18-norsteroids (gonatrienes) of general formula (I), wherein R1, R2, R3, R6, R7, R8, R9, R11, R11?, R14, R15, R15?, R16, R17 and R17? have the meaning cited in the description, and to the use of said compounds as pharmaceutical active ingredients. Said compounds exhibit a high affinity in vitro for estrogen receptor preparations of rat prostate and in an estrogen receptor preparation of rat uterus. Said compounds exhibit in vivo preferential activity on bones as compared to the uterus and/or significant activity with regard to stimulating the expression of 5HT2a-receptors and transporter molecules. The invention also relates to the production of said compounds, therapeutic use and galenic form of said compounds contained in the novel compounds of invention.

Abstract: The invention relates to a new synthesis intermediate product of formula I 1

Abstract: A process is described for the purification of recombinant interleukin-8, which allows the production of interleukin-8 under Good Manufacturing Practice (GMP) conditions.

Abstract: Transformed plants resistant to phenmedipham, which are resistant by having been transformed with a purified and isolated carbamate hydrolase gene. The carbamate hydrolase enzyme produced thereby is responsible for the cleavage of the carbamate bond between the benzene rings of phenmedipham. The invention includes the transformed plants, progeny thereof, transformed plant cells, and method of producing the transformed plants and transformed plant cells, which are resistant to phenmedipham. The invention further includes plasmids comprising the carbamate hydrolase gene capable of inactivating phenmedipham.

Abstract: The present invention relates to novel thrombolitic v-PA's which dissolve blood clots in the human body and thus are suitable for the treatment of cardial infarction, for example.

Abstract: A process for the isolation and characterization of a gene enzyme system for the inactivation of the herbicide phenmedipham, wherein the enzyme is a carbamate hydrolase of Arthrobacter oxidans, which is responsible for the cleavage of the carbamate bond between the benzene rings of phenmedipham. This process includes the isolation of the carbamate hydrolase, the identification of the amino acid sequence of two BrCN cleavage peptides of the carbamate hydrolase, the synthesis of oligonucleotides for specific determination of the carbamate hydrolase sequence by hybridization and identification of the coding region, cloning and specifying the nucleotide sequence of the carbamate hydrolase gene from Arthrobacter oxidans.

Abstract: A process for the isolation and characterization of a gene enzyme system for the inactivation of the herbicide phenmedipham, wherein the enzyme is a carbamate hydrolase of Arthrobacter oxidans, which is responsible for the cleavage of the carbamate bond between the benzene rings of phenmedipham. This process includes the isolation of the carbamate hydrolase, the identification of the amino acid sequence of two BrCN cleavage peptides of the carbamate hydrolase, the synthesis of oligonucleotides for specific determination of the carbamate hydrolase sequence by hybridization and identification of the coding region, cloning and specifying the nucleotide sequence of the carbamate hydrolase gene from Arthrobacter oxidans.

Abstract: A process for the isolation and characterization of a gene enzyme system for the inactivation of the herbicide phenmedipham, wherein the enzyme is a carbamate hydrolase of Arthrobacter oxidans, which is responsible for the cleavage of the carbamate bond between the benzene rings of phenmedipham. This process includes the isolation of the carbamate hydrolase, the identification of the amino acid sequence of two BrCN cleavage peptides of the carbamate hydrolase, the synthesis of oligonucleotides for specific determination of the carbamate hydrolase sequence by hybridization and identification of the coding region, cloning and specifying the nucleotide sequence of the carbamate hydrolase gene from Arthrobacter oxidans.

Abstract: A process for the isolation and characterization of a gene enzyme system for the inactivation of the herbicide phenmedipham, wherein the enzyme is a carbamate hydrolase of Arthrobacter oxidans, which is responsible for the cleavage of the carbamate bond between the benzene rings of phenmedipham. This process includes the isolation of the carbamate hydrolase, the identification of the amino acid sequence of two BrCN cleavage peptides of the carbamate hydrolase, the synthesis of oligonucleotides for specific determination of the carbamate hydrolase sequence by hybridization and identification of the coding region, cloning and specifying the nucleotide sequence of the carbamate hydrolase gene from Arthrobacter oxidans.Plants are transformed with recombinant genes coding for the carbamate hydrolase and transgenic plants which are tolerant to the herbicide are produced.

Abstract: PhoA mutant E. coli SB44, prepared by mutation of E. coli HB101 with an N-nitroso compound, can be used to identify and isolate recombinant plasmids into which a phoA gene has been incorporated. These plasmids can be used to transform bacteria which can be cloned and incubated to provide alkaline phosphatase in high yield. Moreover, these plasmid vectors can be modified in various ways so that the N-terminal amino acid sequence of phoA is followed in reading phase by the DNA coding for some other protein. In turn, these new plasmids can be used to transform bacteria which can be cloned and incubated to produce fusion proteins comprising the desired other protein in high yield and outside of the cell membrane in the periplasmatic space.