Sowmya, P. K. and Mahadesh Prasad, A. J. and Elizabeth, A. F. and D'Souza, C. J. M. (2015) Effect of antibiotics on paraoxonase1: ã-lactamase-like activity of paraoxonase1. Asian Journal Of Biochemical and Pharmaceutical Research, 5 (1). pp. 178-188. ISSN 2249 – 622X
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Paraoxonase1 (PON1), a serum enzyme associated exclusively with High Density Lipoprotein (HDL) is responsible for most of HDLs cardioprotective properties. PON1 activity is a measure of HDL functionality and thus accurate measurement of PON1 activity becomes clinically important. However, factors in the serum like Ca2+, triglycerides, inflammatory cytokines, drugs and environmental toxins might interfere with PON1 measurement. In our current investigation, we have tested the effects of commonly used antibiotics- Tetracycline, Spectinomycin, Gentamicin and Penicillin G on PON1 activity. Tetracycline reduced PON1 activity by 90 at concentration as low as 0.25 mg/ml while the others increased PON1 activity at the same concentration. Upon increasing the concentration of these antibiotics, PON1 activity decreased but not below the control. Because Penicillin G contains a â-lactam ring that resembles lactone ring structure and because PON1 has lactonase activity, we used Penicillin G as a substrate for PON1 and found that Penicillin G was cleaved by PON1. The cleaved product could be separated by TLC and was subjected to 1H-NMR analysis. Penicillin G inhibited the growth of Bacillus subtilis. But upon treatment with PON1, its antibiotic activity was lost. These results suggest that PON1 may have a â-lactamase-like activity in addition to lactonase activity.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PON1 and HDL and Antibiotics and Penicillin G and &beta-Lactamase-Like |
| Subjects: | C Chemical Science > Biochemistry |
| Divisions: | Department of > Biochemistry |
| Depositing User: | Users 19 not found. |
| Date Deposited: | 12 Jul 2019 09:32 |
| Last Modified: | 12 Jul 2019 09:32 |
| URI: | http://eprints.uni-mysore.ac.in/id/eprint/5142 |
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