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Kinetic studies on activation of peptide bond formation by hyaluronic acid.
Theocharis, D A; Drainas, D.
Affiliation
  • Theocharis DA; Laboratory of Biological Chemistry, School of Medicine, University of Patras, Greece.
Int J Biochem ; 24(8): 1341-5, 1992 Aug.
Article in En | MEDLINE | ID: mdl-1644215
ABSTRACT
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.
Subject(s)
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Collection: 01-internacional Database: MEDLINE Main subject: Peptides / Peptidyl Transferases / Hyaluronic Acid Language: En Journal: Int J Biochem Year: 1992 Document type: Article Affiliation country: Grecia
Search on Google
Collection: 01-internacional Database: MEDLINE Main subject: Peptides / Peptidyl Transferases / Hyaluronic Acid Language: En Journal: Int J Biochem Year: 1992 Document type: Article Affiliation country: Grecia