Studies on the fractionation of total transfer ribonucleic acid and purification of an alanine transfer ribonucleic acid from chick embryo.
نویسندگان
چکیده
Chick embryo tRNA, prepared by a simple large-scale method, was fractionated on three different ion-exchange columns. In all cases simple chromatographic patterns for various tRNA species were observed, indicating the presence of only a few major species of tRNA for each amino acid. By repeated chromatography one species of alanine tRNA was purified to approx. 80% purity. T(1) ribonuclease digest of this purified tRNA gave a simple chromatographic pattern. Because of the simplicity of the method of preparation of tRNA from this readily available source and the presence of only a few species of tRNA for each amino acid, chick embryo is suited for the study of tRNA and its various functions in higher systems.
منابع مشابه
Purification of the alanine-, valine-, histidine-, and tyrosine-acceptor ribonucleic acids from yeast.
According to present understanding of the biosynthesis of proteins, the first steps involve activation of the ammo acids (Equation 1) followed by the transfer of the amino acids to specific amino acid-acceptor ribonucleic acids (RNA’s) (Equation 2) (for a recent review see (1)). It is believed that the amino acid-acceptor RNA’s subsequently take part, with the “template” RNA, in determining the...
متن کاملNucleotide Sequences in the Yeast Alanine Transfer Ribonucleic Acid.
The purification of the yeast alanine-, tyrosine-, and valinetransfer ribonucleic acids by countercurrent distribution has been described (l), and preliminary data have been reported on the oligonucleotide compositions of these RNAs (2, 3). The present paper summarizes results of attempts to account quantitatively for all of the fragments obtained by digestion of the alanineRNA with pancreatic ...
متن کاملEvidence for One Leucyl Transfer Ribonucleic Acid Synthetase with Suecificitv for Leucine Transfer Ribonucleic Acids with Different Coding Characteristics*
Leucyl transfer ribonucleic acid synthetase (EC 6.1.1.4, L-leucine: tRNA ligase (AMP)) has been purified from Escherichia coli and is free of other aminoacyl-tRNA synthetases, tRNA-methylating enzymes, and CpCpA-adding enzymes. Several criteria suggest that there is one synthetase with specikity for two forms of leucine-specik tRNA which can be separated by countercurrent distribution: purifica...
متن کاملMultiple forms of lysyl-transfer ribonucleic acid synthetase in Escherichia coli.
Lysyl-transfer ribonucleic acid synthetase (EC 6.1.1.6) was identified as four polypeptide spots after two-dimensional polyacrylamide gel electrophoresis of whole-cell lysates of Escherichia coli. Identification was made by migration with partially purified enzyme preparations, by peptide map patterns, by mutant analysis, and by correlation of spot intensities with changes in enzyme levels unde...
متن کاملViral events necessary for the induction of interferon in chick embryo cells.
Temperature-sensitive mutants of Sindbis virus were employed to investigate the nature of the viral event(s) which induces chick-embryo cells to produce interferon. Chick embryo cells induced by the parental heat-resistant strain of Sindbis virus produced essentially equal amounts of interferon at 29 and 42 C. An RNA(-) and three RNA(+) strains [temperature-sensitive mutants unable (RNA(-)) and...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- The Biochemical journal
دوره 141 3 شماره
صفحات -
تاریخ انتشار 1974