[Isolation, polypeptide composition and properties of aminoacyl-tRNA-synthetase complexes from the rabbit liver]. 1987

A D Vol'fson, and Iu A Motorin, and A F Orlovskiĭ, and K L Gladilin

The procedure for isolation of the aminoacyl-tRNA-synthetase complex from rabbit liver based on the affinity chromatography on heparin- and tRNA-Sepharose has been developed. The complex has a Mr of about 1100 kD and is made up of 10 polypeptides, eight of which are aminoacyl-tRNA synthetase. The complex stability was studied under various conditions. The data obtained are discussed in terms of the involvement of hydrophobic domains of aminoacyl-tRNA synthetases in the stabilization of the complex.

UI MeSH Term Description Entries
D007525 Isoelectric Focusing Electrophoresis in which a pH gradient is established in a gel medium and proteins migrate until they reach the site (or focus) at which the pH is equal to their isoelectric point. Electrofocusing,Focusing, Isoelectric
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D009097 Multienzyme Complexes Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES. Complexes, Multienzyme
D010455 Peptides Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. Peptide,Polypeptide,Polypeptides
D011817 Rabbits A burrowing plant-eating mammal with hind limbs that are longer than its fore limbs. It belongs to the family Leporidae of the order Lagomorpha, and in contrast to hares, possesses 22 instead of 24 pairs of chromosomes. Belgian Hare,New Zealand Rabbit,New Zealand Rabbits,New Zealand White Rabbit,Rabbit,Rabbit, Domestic,Chinchilla Rabbits,NZW Rabbits,New Zealand White Rabbits,Oryctolagus cuniculus,Chinchilla Rabbit,Domestic Rabbit,Domestic Rabbits,Hare, Belgian,NZW Rabbit,Rabbit, Chinchilla,Rabbit, NZW,Rabbit, New Zealand,Rabbits, Chinchilla,Rabbits, Domestic,Rabbits, NZW,Rabbits, New Zealand,Zealand Rabbit, New,Zealand Rabbits, New,cuniculus, Oryctolagus
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
D000604 Amino Acyl-tRNA Synthetases A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS. Amino Acyl T RNA Synthetases,Amino Acyl-tRNA Ligases,Aminoacyl Transfer RNA Synthetase,Aminoacyl-tRNA Synthetase,Transfer RNA Synthetase,tRNA Synthetase,Acyl-tRNA Ligases, Amino,Acyl-tRNA Synthetases, Amino,Amino Acyl tRNA Ligases,Amino Acyl tRNA Synthetases,Aminoacyl tRNA Synthetase,Ligases, Amino Acyl-tRNA,RNA Synthetase, Transfer,Synthetase, Aminoacyl-tRNA,Synthetase, Transfer RNA,Synthetase, tRNA,Synthetases, Amino Acyl-tRNA

Related Publications

A D Vol'fson, and Iu A Motorin, and A F Orlovskiĭ, and K L Gladilin
September 1982, The Journal of biological chemistry,
A D Vol'fson, and Iu A Motorin, and A F Orlovskiĭ, and K L Gladilin
February 1975, Archives of biochemistry and biophysics,
A D Vol'fson, and Iu A Motorin, and A F Orlovskiĭ, and K L Gladilin
July 1981, Proceedings of the National Academy of Sciences of the United States of America,
A D Vol'fson, and Iu A Motorin, and A F Orlovskiĭ, and K L Gladilin
January 1974, Methods in enzymology,
A D Vol'fson, and Iu A Motorin, and A F Orlovskiĭ, and K L Gladilin
March 2015, International journal of molecular sciences,
A D Vol'fson, and Iu A Motorin, and A F Orlovskiĭ, and K L Gladilin
August 2004, Journal of cell science,
A D Vol'fson, and Iu A Motorin, and A F Orlovskiĭ, and K L Gladilin
January 1980, Ukrainskii biokhimicheskii zhurnal (1978),
A D Vol'fson, and Iu A Motorin, and A F Orlovskiĭ, and K L Gladilin
January 1974, Methods in enzymology,
A D Vol'fson, and Iu A Motorin, and A F Orlovskiĭ, and K L Gladilin
January 1988, Ukrainskii biokhimicheskii zhurnal (1978),
Copied contents to your clipboard!