Zobrazeno 1 - 10
of 105
pro vyhledávání: '"C, Coutsogeorgopoulos"'
Publikováno v:
Molecular pharmacology. 53(6)
A detailed kinetic study was carried out on the inhibitory mechanisms of two eukaryotic peptidyltransferase drugs (I), anisomycin and sparsomycin. In an in vitro system from rabbit reticulocytes, AcPhe-puromycin is produced in a pseudo-first-order re
Autor:
S, Kallia-Raftopoulos, D, Synetos, H C, Ottenheijm, L A, van den Broek, C, Coutsogeorgopoulos
Publikováno v:
Molecular pharmacology. 49(6)
The ability of several sparsomycin analogues to inhibit peptide bond formation was studied in vitro. Peptide bonds are formed between puromycin (S) and the acetylPhe-tRNA of acetylPhe-tRNA/70 S ribosome/poly(U) complex (complex C), according to the p
Publikováno v:
Molecular pharmacology. 46(5)
We have investigated the inhibition of peptide bond formation by the antibiotic lincomycin, at 150 mM NH4Cl. We have used an in vitro system in which a ribosomal ternary complex, the acetyl[3H] phenylalanine-tRNA-70 S ribosome-poly(U) complex (comple
Publikováno v:
Journal of Medicinal Chemistry. 18:771-776
Seventeen structural analogs of gougerotin have been compared with the parent compound as inhibitors of the growh of E. coli B and as inhibitors of N-acetylphenylalanylpuromycin formation. The analogs comprise compounds with (1) an intact sarcosyl-D-
Inhibitors of protein synthesis V Irreversible interaction of antibiotics with an initiation complex
Publikováno v:
Nucleic Acids Research. 2:1053-1072
The initiation complex (t-complex) formed in a cell-free system (E. coli) from Ac-Phe-tRNA, poly(U) and washed ribosomes in the presence of initiation factors (ribosomal wash) and GTP, contains the Ac-Phe-tRNA bound quantitatively in a puromycin-reac
Autor:
H. G. Khorana, C. Coutsogeorgopoulos
Publikováno v:
Journal of the American Chemical Society. 86:2926-2932
Publikováno v:
Biochemical and Biophysical Research Communications. 20:129-134
Publikováno v:
Biochemical and Biophysical Research Communications. 5:477-480
An enzyme fraction from calf thymus nuclei which incorporates single ribonucleotides into terminal positions of DNA has been described (1, 2, 3). It has been found that this same enzyme fraction (referred to in this communication as ‘nuclear enzyme
Autor:
C. Coutsogeorgopoulos, R. Fico
Publikováno v:
Biochemical and Biophysical Research Communications. 47:645-651
The reaction of N-Acetyl-phenylalanyl-t-RNA with E.coli ribosomes in the presence of poly Uridylic acid, guanosine 5′-triphosphate, and initiation factors (ribosomal wash), leads to the formation of N-Acetyl-phenylalanyl-RNA-ribosome-poly Uridylic
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects. 55:639-650
The purification of an enzyme fraction from calf-thymus nuclei catalyzing a limited incorporation of deoxyribonucleotides into the terminal positions of DNA has been described. The enzyme studied is apparently distinct from DNA polymerase. The same e