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In vitro enzymological analysis of the recombinant soluble form of SEP demonstrated that it hydrolyzes a variety of vasoactive peptides, including endothelin-1, atrial natriuretic peptide, and angiotensin I. This activity of SEP was inhibited by phosphoramidon and the neutral endopeptidase 24.11 specific inhibitor thiorphan, but it was only partially inhibited by the endothelin-converting enzyme specific inhibitor FR901533. These findings suggest that SEP is a novel metalloprotease that possesses a broad substrate specificity and that it may be involved in the metabolism of biologically active peptides intracellulary as well as extracellularly.

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The result indicates that imprudent use of random urine has a great risk of false evaluation in assessment of the 6beta-hydroxycortisol to cortisol ratio and that the ratio in 24-h urine samples provides a more robust measure of the inter-individual difference of this metabolic ratio, which to a certain but not complete extent represents the CYP3A activity.

Abstract— Carotenoids extracted from the reaction center (RC), the light‐harvesting complex (LH), and the chromatophore membrane of Rhodospirillum rubrum SI were analyzed by high‐performance liquid chromatography. The chemical structures and the configurations of major components were determined by means of mass, Raman, electronic absorption and 1H‐NMR spectroscopy. The results indicated: (1) 15‐cis‐spirilloxanthin is bound to RC; (2) both all‐frans‐spirilloxanthin and aII‐(ran.s‐3,4‐dihydrospirilloxanthin are bound to LH and (3) 13‐cK‐spirilloxanthin is additionally present in the chromatophore membrane. The natural selection of the carotenoid configurations, i.e. 15‐ris by RC and aW‐trans by LH, is discussed in relation to the physiological functions and the photophysical properties of isomeric carotenoids.