Extrahepatic Microsomal Forms: Lung Microsomal Cytochrome P450 Isozymes

Arınç, Emel

doi:10.1007/978-3-642-77763-9_24

Cited by 6 publications

(4 citation statements)

References 31 publications

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“…Immunoblot analysis of purified sheep lung CYP2B and PB-induced rabbit liver and lung CYP2B4 using the antibodies raised against sheep lung CYP2B showed that these cytochromes were homologous [41,42]. Similar results were also obtained when purified sheep lung CYP2B and rabbit liver CYP2B4 were probed with anti-rabbit liver P4502B4 [43,44]. The fractions obtained during purification of CYP2B-like protein were subjected to SDS-PAGE as described before and separated proteins were then transferred from gel to a nitrocellulose membrane by using the trans-blot electrophoretic transfer cell (Bio-Rad) containing Tris-glycine buffer, pH 8.3, and methanol, at 90 V (400 mA).…”

Section: Western Blot Analysissupporting

confidence: 71%

“…It gave one protein band on SDS-PAGE. The apparent molecular weight was calculated to be 49,300 Da, which is very similar to that of rabbit liver and lung CYP2B4 and sheep lung CYP2B (49,500 Da) [43,44,47]. Immunoblot analysis of purified sheep lung CYP2B and PB-induced rabbit liver and lung CYP2B4 showed that these cytochromes were homologous [41][42][43]47].…”

Section: Discussionmentioning

confidence: 99%

“…The purified CYP was very active in the metabolism of benzphetamine similar to the purified CYP2Bs from sheep lung, rabbit, and rat liver [41][42][43][44][47][48][49]. The purified mullet CYP also catalyzed O-depenthylation of pentoxyresorufin known to be metabolized by CYP2B and N-demethylation of ethylmorphine and cocaine; known to be catalyzed by cytochrome CYP2B and CYP3A [21,43,44,46,[50][51][52]. Although cytochrome P4503A catalyzes erythromycin N-demethylation reaction in mammals, reconstitution studies showed that the purified CYP2B-like protein also catalyzed Ndemethylation of erythromycin.…”

Section: Discussionmentioning

confidence: 99%

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Purification of CYP2B‐like protein from feral leaping mullet (Liza saliens) liver microsomes and its biocatalytic, molecular, and immunological characterization

Bozcaarmutlu

Arınç

2008

J Biochem & Molecular Tox

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In this study, CYP2B-immunoreactive protein was purified to electrophoretic homogeneity from the liver microsomes of leaping mullet. The purified cytochrome P450 (CYP) gave a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis having a M(r) of 49,300 Da. Absolute absorption spectrum of the purified CYP showed a maximum at 417 nm and CO-difference spectrum of dithionite-reduced cytochrome P450 gave a peak at 450 nm. The purified CYP was found to be active in N-demethylation of benzphetamine, erythromycin, and ethylmorphine, and O-dealkylation of pentoxyresorufin in the reconstituted system. However, it was unable to catalyze O-dealkylation of ethoxyresorufin, methoxyresorufin, benzyloxyresorufin, and hydroxylation of lauric acid and aniline. The purified CYP showed strong cross-reactivity with anti-sheep lung CYP2B, a homologue of CYP2B4. N-terminal amino acid sequence of the mullet P450 had the highest degree of homology with CYP2Bs among the known CYPs. Spectral, electrophoretic, immunochemical, N-terminal amino acid sequence, and biocatalytic properties of the purified CYP are most similar to those of mammalian cytochrome P4502B. All these data indicate that the purified CYP is certainly 2B-like. In this study, we not only purified biocatalytically active CYP2B-like protein from fish, but also demonstrated detailed functional properties of CYP2B-like protein for the first time.

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Section: Western Blot Analysissupporting

confidence: 71%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Purification of CYP2B‐like protein from feral leaping mullet (Liza saliens) liver microsomes and its biocatalytic, molecular, and immunological characterization

Bozcaarmutlu

Arınç

2008

J Biochem & Molecular Tox

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“…La localización de esta hemoproteína es ubícua, y aunque el hígado de mamíferos comprende el mayor porcentaje de citocromo P-450, se han encontrado pequeñas cantidades de P-450 en tejidos extrahepáticos tales como: riñón, pulmón, tracto gastro-intestinal, cerebro, epitelio nasal, pancreas, bazo, testículos y ovario (Arinc, 1993;Strobel y cols., 1993; músculo esquelético (Guengerich, 1993). Las mitocondrias del hígado, del riñón y, especialmente de las glándulas endocrinas, que metabolizan hormonas esteroides, contienen P-450.…”

Section: Sistema Citocromo P-450unclassified