Kinetic studies on activation of peptide bond formation by hyaluronic acid.
1. In this study, a cell-free system derived from Escherichia coli has been used in order to examine in detail the effect of hyaluronic acid on peptide bond formation with the aid of puromycin reaction. 2. This reaction is activated by hyaluronic acid. 3. The degree of activation of peptide bond formation depends on the molecular size of hyaluronic acid. 4. The kinetic analysis revealed that the hyaluronic acid acts as a mixed-type nonessential activator. 5. The presence of hyaluronic acid improves about 9-fold the activity status of ternary complex as it can be calculated by k3/k5 ratio.
Theocharis
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Laboratory of Biological Chemistry, School of Medicine, University of Patras, Greece.
Drainas
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D004926:Escherichia coli / Q000378:metabolism; D006820:Hyaluronic Acid / Q000494:pharmacology*; D006821:Hyaluronoglucosaminidase / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D010455:Peptides / Q000378:metabolism*; D010458:Peptidyl Transferases / Q000378:metabolism*; D011072:Poly U / Q000378:metabolism; D011691:Puromycin / Q000378:metabolism; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism
D010455:Peptides; D012346:RNA, Transfer, Amino Acyl; C006383:tRNA, N-acetylphenylalanine-; D011072:Poly U; D011691:Puromycin; D006820:Hyaluronic Acid; D010458:Peptidyl Transferases; D006821:Hyaluronoglucosaminidase