Peptide chain elongation: indications for the binding of an amino acid polymerization factor, guanosine 5'-triphosphate-aminoacyl transfer ribonucleic acid complex to the messenger-ribosome complex

Biochemistry ◽  
1970 ◽  
Vol 9 (3) ◽  
pp. 508-514 ◽  
Author(s):  
Arthur Skoultchi ◽  
Yasushi Ono ◽  
John Waterson ◽  
Peter Lengyel
Keyword(s):  
Amino Acid ◽  
Ribonucleic Acid ◽  
Peptide Chain ◽  
Chain Elongation ◽  
Acid Complex ◽  
Aminoacyl Transfer

scholarly journals Preparation of polyribosome aminoacyl-transfer ribonucleic acid from the muscle of chick embryos.

1975 ◽  
Vol 147 (3) ◽  
pp. 473-477 ◽  
Author(s):  
M Nwagwu
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Sodium Dodecyl Sulphate ◽  
Ribonucleic Acid ◽  
Free Amino Acids ◽  
Free Amino ◽  
Sodium Dodecyl ◽  
Specific Radioactivity ◽  
Chick Embryos ◽  
Aminoacyl Transfer

A procedure for preparing polyribosome aminoacyl-tRNA free from contamination by supernatant aminoacyl-tRNA and free amino acids is described. Important features of the procedure are the use of acidic buffers to help protect the amino acid-tRNA linkage and the inclusion of sodium dodecyl sulphate, to inhibit ribonuclease activity. The specific radioactivity of polyribosome aminoacyl-tRNA is high within 30s and reaches a maximum in 2 1/2 min, well ahead of polyribosome peptides which, as described by Herrmann et al. (1971), attain maximum specific radioactivity in about 10 min.

scholarly journals Myocardial aminoacyl-transfer-ribonucleic acid synthetase and aminoacyl-transferring enzyme activity

1972 ◽  
Vol 126 (2) ◽  
pp. 409-416 ◽  
Author(s):  
K. Gibson ◽  
P. Harris
Keyword(s):  
Enzyme Activity ◽  
Amino Acid ◽  
Ribonucleic Acid ◽  
Trna Synthetase ◽  
Transferase Activity ◽  
Synthetase Activity ◽  
Aminoacyl Trna Synthetase ◽  
Standard Preparation ◽  
Enzyme Systems ◽  
Aminoacyl Transfer

The properties of cytoplasmic aminoacyl-tRNA synthetase and aminoacyl-transferring enzymes in the myocardium were examined and methods for the assay of the activity of these enzyme systems were developed. Aminoacyl-tRNA synthetase activity was measured from the rate of incorporation of 14C-labelled amino acid into aminoacyl-tRNA. Transferase activity was measured from the rate of incorporation of amino[14C]acyl-tRNA into protein in the presence of a standard preparation of hepatic ribosomes. Aminoacyl-tRNA synthetase activity is labile once the heart has been homogenized, whereas transferase activity is stable. The source of energy for synthetase activity is ATP; that for transferase is GTP. Transferase activity was inhibited by puromycin and stimulated by dithiothreitol, whereas synthetase activity was unaffected.

Convergent peptide synthesis

1999 ◽  
Author(s):  
Kleomenis Barlos ◽  
Dimitrios Gatos
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Peptide Synthesis ◽  
Solid Phase ◽  
Peptide Chain ◽  
Chain Elongation ◽  
Peptide Fragments ◽  
Terminal Amino Acid ◽  
Convergent Synthesis ◽  
Terminal Amino

Besides the classical step-by-step synthesis, the convergent solid phase peptide synthesis (CSPPS) was developed for the preparation of complex and difficult peptides and small proteins. According to this method, suitably protected peptide fragments spanning the entire peptide sequence and prepared on the solid phase are condensed, either on a solid support or in solution, to the target peptide. Convergent synthesis is reviewed in recent publications. In this chapter, full experimental details are given for the preparation of complex peptides by applying convergent techniques, using 2-chlorotrityl chloride resin (CLTR) and Fmoc-amino acids. In the step-by-step peptide chain elongation the resin-bound C-terminal amino acid is reacted sequentially with suitably protected and activated amino acids. The peptide is thus elongated steadily towards the N-terminal direction. This is advantageous over the opposite direction where the elongation is performed from the N- to the C-terminus, because in the second case the growing peptide is activated at the C-terminal amino acid, which leads to its extensive racemization. This limits considerably the synthetic possibilities of the method. In convergent synthesis, no directional restrictions exist and the chain elongation can be performed with equal possibility to be successful to any direction. Figure 1 describes schematically the C- to N-terminal synthesis which is the most studied to date. The strategies where the synthesis begins from a central fragment and the peptide chain is extended to both C- and N-terminal directions and from the N-terminal towards the C-terminal can be considered, at the present time, to be in its infancy. In general, protected peptide fragments of any length can be used in the condensation reaction, if they are of satisfactory purity and solubility. Usually, fragments of up to 15 amino acids in length are used, because of their simpler purification by RP-HPLC compared with the longer peptides. The solubility of protected peptide acids is independent of their length. The selection of the correct fragments is very important for the success of convergent synthesis. It is helpful to analyse all available structural information, determined or calculated, for the target peptide. Peptide regions where β-turns are known to occur are readily identified as ‘difficult’ sequences during their synthesis.

Peptide Chain Elongation: Discrimination against the Initiator Transfer RNA by Microbial Amino-acid Polymerization Factors

Nature ◽  
1968 ◽  
Vol 220 (5174) ◽  
pp. 1304-1307 ◽  
Author(s):  
YASUSHI ONO ◽  
ARTHUR SKOULTCHI ◽  
ALBRECHT KLEIN ◽  
PETER LENGYEL
Keyword(s):  
Amino Acid ◽  
Transfer Rna ◽  
Peptide Chain ◽  
Chain Elongation
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