Induction of Cytochrome P4501A1 by beta-naphthoflavone and determination of enzyme properties in Huso huso
Cytochrome P4501A1 is a major isoenzyme in fish monooxygenase system which is induced by polycyclic aromatic hydrocarbons (PAHs) compounds. In this research, the inducing effect of p-naphthoflavone and its catalytic properties was studied in Huso huso liver. Fish were given ip injection of p-naphtho...
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| Format: | Article |
| Language: | fas |
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Iranian Fisheries Research Organization
2005-01-01
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| Series: | Majallah-i ̒Ilmī-i Shīlāt-i Īrān |
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| Online Access: | http://isfj.areo.ir/article_113837_en.html |
| _version_ | 1828372444976513024 |
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| author | K. Karimzadeh1; A. Mostafaei2; A. Esmaeili sari3; M. Porkazemi1; A. Zahmatkesh1 |
| author_facet | K. Karimzadeh1; A. Mostafaei2; A. Esmaeili sari3; M. Porkazemi1; A. Zahmatkesh1 |
| author_sort | K. Karimzadeh1; A. Mostafaei2; A. Esmaeili sari3; M. Porkazemi1; A. Zahmatkesh1 |
| collection | DOAJ |
| description | Cytochrome P4501A1 is a major isoenzyme in fish monooxygenase system which is induced by polycyclic aromatic hydrocarbons (PAHs) compounds. In this research, the inducing effect of p-naphthoflavone and its catalytic properties was studied in Huso huso liver. Fish were given ip injection of p-naphthoflavone at three different doses. The enzyme activity was measured with de-ethylation of ethoxyresorufin reaction (EROD) by flourometery method and relative amount of induced proteins were determined using polyacrylamide gel electrophoresis (SDS-PAGE). The results showed that EROD activity in the microsomal fraction of the treated fish was 15-26 folds that of the control group. Optimum activity of this enzyme was observed at 20-25 degrees centigrade. The maximum enzyme activity was seen in the presence of 180 micrograms of microsomal protein and 1.53BM of 7-ethoxyresorufin. SDS-PAGE of microsomal protein pattern in the treated fish revealed a protein with molecular mass I K Da translating to cytochrome P4501A. We conclude that the p-naphthoflavone in fish liver can induce cytochrome P4501A gene and increase its biosynthesis leading to raised enzyme activity in EROD reaction. |
| first_indexed | 2024-04-14T07:03:44Z |
| format | Article |
| id | doaj.art-772375de80d14a6190876a3d2caeea72 |
| institution | Directory Open Access Journal |
| issn | 1026-1354 2322-5998 |
| language | fas |
| last_indexed | 2024-04-14T07:03:44Z |
| publishDate | 2005-01-01 |
| publisher | Iranian Fisheries Research Organization |
| record_format | Article |
| series | Majallah-i ̒Ilmī-i Shīlāt-i Īrān |
| spelling | doaj.art-772375de80d14a6190876a3d2caeea722022-12-22T02:06:39ZfasIranian Fisheries Research OrganizationMajallah-i ̒Ilmī-i Shīlāt-i Īrān1026-13542322-59982005-01-01142115126Induction of Cytochrome P4501A1 by beta-naphthoflavone and determination of enzyme properties in Huso husoK. Karimzadeh1; A. Mostafaei2; A. Esmaeili sari3; M. Porkazemi1; A. Zahmatkesh1Cytochrome P4501A1 is a major isoenzyme in fish monooxygenase system which is induced by polycyclic aromatic hydrocarbons (PAHs) compounds. In this research, the inducing effect of p-naphthoflavone and its catalytic properties was studied in Huso huso liver. Fish were given ip injection of p-naphthoflavone at three different doses. The enzyme activity was measured with de-ethylation of ethoxyresorufin reaction (EROD) by flourometery method and relative amount of induced proteins were determined using polyacrylamide gel electrophoresis (SDS-PAGE). The results showed that EROD activity in the microsomal fraction of the treated fish was 15-26 folds that of the control group. Optimum activity of this enzyme was observed at 20-25 degrees centigrade. The maximum enzyme activity was seen in the presence of 180 micrograms of microsomal protein and 1.53BM of 7-ethoxyresorufin. SDS-PAGE of microsomal protein pattern in the treated fish revealed a protein with molecular mass I K Da translating to cytochrome P4501A. We conclude that the p-naphthoflavone in fish liver can induce cytochrome P4501A gene and increase its biosynthesis leading to raised enzyme activity in EROD reaction.http://isfj.areo.ir/article_113837_en.htmlCytochrome P4501AI; Beta-naphtho flavone; Huso huso. Iran |
| spellingShingle | K. Karimzadeh1; A. Mostafaei2; A. Esmaeili sari3; M. Porkazemi1; A. Zahmatkesh1 Induction of Cytochrome P4501A1 by beta-naphthoflavone and determination of enzyme properties in Huso huso Majallah-i ̒Ilmī-i Shīlāt-i Īrān Cytochrome P4501AI; Beta-naphtho flavone; Huso huso. Iran |
| title | Induction of Cytochrome P4501A1 by beta-naphthoflavone and determination of enzyme properties in Huso huso |
| title_full | Induction of Cytochrome P4501A1 by beta-naphthoflavone and determination of enzyme properties in Huso huso |
| title_fullStr | Induction of Cytochrome P4501A1 by beta-naphthoflavone and determination of enzyme properties in Huso huso |
| title_full_unstemmed | Induction of Cytochrome P4501A1 by beta-naphthoflavone and determination of enzyme properties in Huso huso |
| title_short | Induction of Cytochrome P4501A1 by beta-naphthoflavone and determination of enzyme properties in Huso huso |
| title_sort | induction of cytochrome p4501a1 by beta naphthoflavone and determination of enzyme properties in huso huso |
| topic | Cytochrome P4501AI; Beta-naphtho flavone; Huso huso. Iran |
| url | http://isfj.areo.ir/article_113837_en.html |
| work_keys_str_mv | AT kkarimzadeh1amostafaei2aesmaeilisari3mporkazemi1azahmatkesh1 inductionofcytochromep4501a1bybetanaphthoflavoneanddeterminationofenzymepropertiesinhusohuso |