Optical probe for the cytochrome P-450 cholesterol side chain cl

Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving cholesterol

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435189, C12Q 160, C12N 902

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active

051107252

ABSTRACT:
An optical probe enables the study of enzyme activity by absorbance spectroscopy or by sensitive fluorescence methods. In particular, the probe provides the ability to monitor the activity of cytochrome P-450.sub.scc enzyme, the rate limiting enzyme for steroid biosynthesis. Located on the inner mitochondrial membrane, P-450.sub.scc catalyzes the conversion of cholesterol to pregnenolone and isocapraldehyde by sequential oxidations of the cholesterol side chain. The fluorogenic probe includes a cholesterol-like steroid linked to a chromophore through a linking group. The chromophore is selected to have little optical response when linked to the steroid substrate and an enhanced optical response when cleaved from the substrate and linking group. Thus, a fluorescent anion that can be optically detected is generated by the side-chain cleavage reaction during steroidogenesis.

REFERENCES:
R. B. Hochberg et al., "A Simple and Precise Assay of the Enzymatic Conversion of Cholesterol into Pregnenolone", 13 Biochem. No. 3, pp. 603-608 (1974).
N. B. Goldring et al., "Immunofluorescent Probing of the Mitochondrial Cholesterol Side-Chain Cleavage Cytochrome P-450 Expressed in Differentiating Granulossa Cells in Culture", 119 Endocrinology, No. 6, pp. 2821-2832 (1986).
J. D. Lambeth, "Cytochrome P-450.sub.scc --A Review of the Specificity and Properties of the Cholesterol Binding Site", 12 Endocrine Research, No. 4, pp. 371-392 (1986).
Kao et al., Biochemistry 17:2689-2696 (78).
Drew, J. et al., J. Org. Chem. 52:4047-4052 (87), Synthesis from Pregnenolone of Fluorescent Cholesterol Analogue Probes with Conjugated Unsaturation in the Side Chain.
Babb, B. et al., CA 109(1):3045Y (87), Hydrolyzable Fluorescent Substrates and Analytical Determinations of Enzymes Using Same.

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