Structure and Function of Transfer Ribonucleic Acid
نویسندگان
چکیده
منابع مشابه
Structure and function of transfer ribonucleic acid. 3. Some properties of a complex between valyl transfer ribonucleic acid synthetase and transfer ribonucleic acid specific for valine.
The formation and some properties of a stable complex between valyl transfer ribonucleic acid synthetase and transfer RNA from yeast have been investigated by three different methods for the isolation of the complex: titration over Sephadex, sucrose gradient centrifugation, and electrophoresis on Pevikon as supporting medium. Transfer RNA specific for valine (tRNAvsl) can be separated into two ...
متن کاملStructure and function of transfer ribonucleic acid. IV. Complexes between valyl transfer ribonucleic acid synthetase and structurally modified transfer ribonucleic acid specific for valine.
The formation of a stable complex between valyl transfer ribonucleic acid synthetase from yeast and transfer RNA specific for valine (tRNAVa’) from the same source has been used as a model for the recognition between enzyme and tRNA. With the use of sucrose gradient centrifugation to isolate the complex, the major fraction of tRNAVal (tRNAp’) was found to retain its ability to form a stable com...
متن کاملThe Function of Pseudouridylic Acid in Transfer Ribonucleic Acid II. INHIBITION OF AMINO ACYL TRANSFER RIBONUCLEIC ACID-RIBOSOME COMPLEX FORMATION
Inhibition of the nonenzymatic binding of phenylalanyl transfer RNA to polyuridylic acid-coded ribosomes at 20 mu magnesium was used as an assay to determine whether the tetranucleotide ribothymidylyl-pseudouridylyl-cytidylyl-guanosine 3’-phosphate possessed any specific ability to bind to ribosomes. Inhibition of binding at the peptidyl site was studied by adding tetracycline to block aminoacy...
متن کاملHuman tryptophan transfer ribonucleic acid synthetase. Composition, function of thiol groups, and structure of thiol peptides.
Human tryptophanyl-tRNA synthetase resembles its counterpart in Escherichia coli in quaternary structure (alpha2), but differs in molecular weight, amino acid composition, the number of thiol groups, and the relationship of the thiol groups to enzyme activity. Nevertheless, one of the thiol groups resides in a heptapeptide sequence homologous to a heptapeptide sequence containing a thiol group ...
متن کاملTransfer ribonucleic acid nucleotidyltransferase and transfer ribonucleic acid in Sendai virions.
Sendai virions contain both transfer ribonucleic acid (tRNA) nucleotidyltransferase and its substrate, tRNA missing its CCA-OH end.
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1969
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)78246-5