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Results 1 - 7 of 7
EC Number
examination of protein-membrane interactions between P450scc and its redox partners on 1,2-dimyristoyl-sn-glycero-3-phosphocholine membranes containing cholesterol (20%), using a quartz crystal microbalance with dissipation monitoring
the development of a cholesterol biosensor based on screen-printed electrodes modified with multi-walled carbon nanotubes and with the cytochromes P450scc may ensure a high sensitivity. Role of the nanotubes in mediating electron transfer to the cytochrome P450scc is verified as further improved with respect to the case of rhodium-graphite electrodes modified by the use of gold nanoparticles
drug development
the vitamin D3 derivatives produced by the action of P450scc are good candidates for use in the therapy of hyperproliferative disorders
P450scc overexpression in the ventral tegmental area significantly reduces ethanol self-administration of alcohol preferring rats trained to self-administer ethanol, by 20% over the 3 week test period. P450scc overexpression in the nucleus accumbens, does not alter ethanol self-administration. P450scc overexpression produces a 36% increase in (3alpha,5alpha)-3-hydroxypregnan-20-one-positive cells in the ventral tegmental area, but does not increase (3alpha,5alpha)-3-hydroxypregnan-20-one immunoreactivity in nucleus accumbens
significant inversed statistical correlation of enzyme immunoreactivity with residual size of tumor in epithelial ovarian carcinoma, but correlation is not an independent prognostic value
treatment of certain hormone-related pathologies
construction of a fusion protein consisting of cytochrome P450scc (CYP11A1), adrenodoxin and adrenodoxin reductase including 2A peptide from Picornaviridae which is capable of self-cleavage. Introduction to Escherichia coli leads to a high level of expression but no cleavage. In yeast Saccharomyces cerevisiae, the discrete proteins P450scc-2A, adrenodoxin-2A and adrenodoxin reductase are expressed, with a significant proportion present in a fusion adrenodoxin-2A-adrenodoxin reductase. The enzyme system is catalytically active
Results 1 - 7 of 7