Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Charalambos Coutsogeorgopoulos"'
Publikováno v:
European Journal of Biochemistry. 9/1/89, Vol. 184 Issue 1, p47-52. 6p.
Publikováno v:
Journal of Enzyme Inhibition. 12:79-99
A systematic procedure for the kinetic study of irreversible inhibition when the enzyme is consumed in the reaction which it catalyses, has been developed and analysed. Whereas in most reactions the enzymes are regenerated after each catalytic event
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac29df12033db0d7abcd50a772673d9a
https://doi.org/10.3109/14756369709035811
https://doi.org/10.3109/14756369709035811
Publikováno v:
Biochemistry. 31:5861-5868
Before CI isomerizes to C*I, we detect a competitive phase of inhibition (Ki = k5/k4 = 0.05 microM) which eventually, by increasing the concentration of I, becomes linear mixed noncompetitive and involves C*I in place of CI. The equilibration of C an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4365855aef04a43a4f78eedb7ca63ca
https://doi.org/10.1021/bi00140a023
https://doi.org/10.1021/bi00140a023
Publikováno v:
Biochimica et biophysica acta. 1342(2)
The effect of NH4+ and K+ ions on the activity of ribosomal peptidyltransferase was investigated in a model system derived from Escherichia coli, in which AcPhe-puromycin is produced by a pseudo-first-order reaction between the preformed AcPhe-tRNA-p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56062330b660a9adc8d76e171ffdd439
https://pubmed.ncbi.nlm.nih.gov/9392527
https://pubmed.ncbi.nlm.nih.gov/9392527
Publikováno v:
Archives of biochemistry and biophysics. 345(2)
In an effort to elucidate the role of potassium ions in the formation of peptide bond, we have used the reaction between puromycin and a ribosomal complex (from rabbit reticulocytes) bearing the donor substrate, AcPhe-tRNA, prebound at the so-called
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f7a8f4a4cfb0035694c4d54a8ff6327
https://pubmed.ncbi.nlm.nih.gov/9308906
https://pubmed.ncbi.nlm.nih.gov/9308906
Publikováno v:
Analytical biochemistry. 247(1)
We have developed an in vitro system for the determination of peptidyltransferase activity in rabbit reticulocyte ribosomes. Using this system, a detailed kinetic analysis of a model reaction for peptidyltransferase is described, with AcPhe-tRNA as t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3623638fa86b0362ac929637de499746
https://pubmed.ncbi.nlm.nih.gov/9126380
https://pubmed.ncbi.nlm.nih.gov/9126380
Publikováno v:
Biochemistry. 32(40)
The inhibition of peptide bond formation by spiramycin was studied in an in vitro system derived from Escherichia coli. Peptide bonds are formed between puromycin (S) and Ac-Phe-tRNA, which is a component of complex C, i.e., of the [Ac-Phe-tRNA-70S r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::265962caf31adb020749b8913467b104
https://pubmed.ncbi.nlm.nih.gov/8399209
https://pubmed.ncbi.nlm.nih.gov/8399209
Publikováno v:
Archives of biochemistry and biophysics. 298(2)
In a system derived from Escherichia coli, we carried out a detailed kinetic analysis of the inhibition of the puromycin reaction by lincomycin. N-Acetylphenylalanyl-tRNA (Ac-Phe-tRNA; the donor) reacts with excess puromycin (S) according to reaction
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::638cc98ff8acd4949c2302bc9dab3512
https://pubmed.ncbi.nlm.nih.gov/1416965
https://pubmed.ncbi.nlm.nih.gov/1416965
Autor:
Dimitrios L. Kalpaxis, Charalambos Coutsogeorgopoulos, Dimitrios A. Theocharis, Denis Drainas, Dennis Synetos
Publikováno v:
Archives of biochemistry and biophysics. 292(1)
A cell-free system derived from Escherichia coli has been used in order to study the kinetics of inhibition of peptide bond formation with the aid of the puromycin reaction in solution. A similar study has been carried out earlier on a solid support
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64b81da39e90362fb669f23848fda215
https://pubmed.ncbi.nlm.nih.gov/1727642
https://pubmed.ncbi.nlm.nih.gov/1727642
Publikováno v:
European Journal of Biochemistry. 184:47-52
The puromycin reaction, catalyzed by the ribosomal peptidyltransferase, has been carried out so as to make the definition of two distinct parameters of this reaction possible. These are (a) the final degree of the reaction which gives the proportion
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f19d8008aec74da4c5cb7e5b49332973
https://doi.org/10.1111/j.1432-1033.1989.tb14988.x
https://doi.org/10.1111/j.1432-1033.1989.tb14988.x