| dc.creator |
GÖKÇE, Başak |
|
| dc.creator |
Bytyqi-Damoni, Arlinda |
|
| dc.creator |
Genc, Hayriye |
|
| dc.creator |
Zengin, Mustafa |
|
| dc.creator |
Gencer, Nahit |
|
| dc.creator |
Arslan, Oktay |
|
| dc.date |
2016-12-31T21:00:00Z |
|
| dc.date.accessioned |
2020-10-06T10:24:24Z |
|
| dc.date.available |
2020-10-06T10:24:24Z |
|
| dc.identifier |
5d5be6f5-1d95-43fb-b26c-008a0e1a8c04 |
|
| dc.identifier |
https://avesis.sdu.edu.tr/publication/details/5d5be6f5-1d95-43fb-b26c-008a0e1a8c04/oai |
|
| dc.identifier.uri |
http://acikerisim.sdu.edu.tr/xmlui/handle/123456789/61242 |
|
| dc.description |
Paraoxonase 1 (PON1) is an antioxidant enzyme associated with high-density lipoproteins (HDL). PON1 has the ability to inhibit lipid peroxides and to hydrolyze a wide variety of substrates such as esters, thioesters, phosphotriesterases, carbonates, lactones and thio lactones. We hypothesized that whether paraoxonase hydrolyses some carbazole P-lactam compounds or not. For this purpose, human serum paraoxonase (hPON1) was purified from human serum blood via two step procedure by using ammonium sulphate precipitation and sepharose-4B-L-tyrosinel-napthylamine-chromatograpy. The in vitro effects of P-lactam compounds on paraoxonase 1 (PON1) were investigated using paraoxon substrate. The results showed that carbazole P-lactam derivatives positively modulated paraoxonase enzyme activity. Among the compounds, 3g and 3h on PON enzyme were found to be the most powerful activators. |
|
| dc.language |
eng |
|
| dc.rights |
info:eu-repo/semantics/closedAccess |
|
| dc.title |
IMPACT OF CARBAZOLE P-LACTAM DERIVATIVES ON PARAOXONASE-1 ACTIVITY |
|
| dc.type |
info:eu-repo/semantics/article |
|