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Biomedical subjects

I Rychlík

Publications and source records attributed to I Rychlík.

At least 91 records · Page 5Linked to original sources
PubMed1976

Effect of the leucomycin-like macrolide antibiotic turimycin on ribosomal peptidyltransferase from Eschericha coli.

The relationship between the effect of different turimycin components on ribosomal peptidyltransferase of E. coli, antimicrobial activity and chemical structure were studied. Inhibition of peptidyltransferase as well as antimicrobial activity increased with the length of the aliphatic side chain in 4''-position of mycarose and decreased with acylation in 3-position of the lactone ring. Inhibition of peptidyltransferase is paralleled by inhibition of acceptor substrate binding.

Acyltransferases↗
PubMed1975

Milk-ejecting and uterotonic activities of oxytocin analogues in rats.

The milk-ejecting activity of oxytocin analogues modified in the aminoterminal part of the molecule was determined in experiment on rats in vivo. As compared with oxytocin, the analogues did not have significantly higher milk-ejecting activity and there was no dissociation of the two basic oxytocin-like activities.

Animals↗
PubMed1974

The role of aminoacyl-tRNA binding site on the factor EF-T in uncoupled GTPase reaction.

The properties of the N-tosyl-L-phenylalanyl chloromethane treated EF-T factor were studied in a ribosomal system in which splitting of GTP occurs. The action of N-tosyl-L-phenylalanyl chloromethane inhibits the binding of aminoacyl-tRNA to the EF-T factor. The binding and exchange of guanosine phosphates continued to be preserved. The inhibited factor is inactive in the GTPase reaction which depends on the participation of ribosomes and aminoacyl-tRNA. The uncoupled GTPase reaction (which is not dependent on the presence of aminoacyl-tRNA) is also sensitive to the effect of the inhibitor. The inhibition of the uncoupled GTPase is incomplete. These findings are attributed to the involvement of the aminoacyl-tRNA binding site of the EF-T factor in the uncoupled GTPase reaction.

Binding Sites↗