BIOMAT Database Logo BIOMAT Database Logo

Triose-phosphate isomerase from Pyrococcus woesei and Methanothermus fervidus. 2001

A Schramm, and M Kohlhoff, and R Hensel
Universität Essen, Essen 45117, Germany.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D002850 Chromatography, Gel Chromatography on non-ionic gels without regard to the mechanism of solute discrimination. Chromatography, Exclusion,Chromatography, Gel Permeation,Chromatography, Molecular Sieve,Gel Filtration,Gel Filtration Chromatography,Chromatography, Size Exclusion,Exclusion Chromatography,Gel Chromatography,Gel Permeation Chromatography,Molecular Sieve Chromatography,Chromatography, Gel Filtration,Exclusion Chromatography, Size,Filtration Chromatography, Gel,Filtration, Gel,Sieve Chromatography, Molecular,Size Exclusion Chromatography
D002852 Chromatography, Ion Exchange Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins. Chromatography, Ion-Exchange,Ion-Exchange Chromatography,Chromatographies, Ion Exchange,Chromatographies, Ion-Exchange,Ion Exchange Chromatographies,Ion Exchange Chromatography,Ion-Exchange Chromatographies
D004795 Enzyme Stability The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat. Enzyme Stabilities,Stabilities, Enzyme,Stability, Enzyme
D006358 Hot Temperature Presence of warmth or heat or a temperature notably higher than an accustomed norm. Heat,Hot Temperatures,Temperature, Hot,Temperatures, Hot
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013379 Substrate Specificity A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts. Specificities, Substrate,Specificity, Substrate,Substrate Specificities

Related Publications

A Schramm, and M Kohlhoff, and R Hensel
Triose phosphate isomerase from Bacillus stearothermophilus.
October 1971, The Biochemical journal,
A Schramm, and M Kohlhoff, and R Hensel
Archaeal nucleosome positioning sequence from Methanothermus fervidus.
June 1999, Journal of molecular biology,
A Schramm, and M Kohlhoff, and R Hensel
Mitochondrial triose phosphate isomerase.
January 1960, Biochimica et biophysica acta,
A Schramm, and M Kohlhoff, and R Hensel
Triose phosphate isomerase deficiency.
October 1977, Biochemical medicine,
A Schramm, and M Kohlhoff, and R Hensel
Preliminary crystallographic studies of triosephosphate isomerase (TIM) from the hyperthermophilic Archaeon Pyrococcus woesei.
November 1998, Acta crystallographica. Section D, Biological crystallography,
A Schramm, and M Kohlhoff, and R Hensel
Di-myo-inositol-1,1'-phosphate: a new inositol phosphate isolated from Pyrococcus woesei.
July 1992, FEBS letters,
A Schramm, and M Kohlhoff, and R Hensel
Refolding of triose phosphate isomerase.
September 1973, The Biochemical journal,
A Schramm, and M Kohlhoff, and R Hensel
Proteopedia entry: triose phosphate isomerase.
January 2011, Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology,
A Schramm, and M Kohlhoff, and R Hensel
Kinetics of triose phosphate isomerase.
March 1968, Biochimica et biophysica acta,
A Schramm, and M Kohlhoff, and R Hensel
Purification and characterization of D-glyceraldehyde-3-phosphate dehydrogenase from the thermophilic archaebacterium Methanothermus fervidus.
May 1987, European journal of biochemistry,
Copied contents to your clipboard!