Background: The ubiquitously expressed dipeptidyl peptidase 3 (DPP3) is involved in protein metabolism, blood pressure regulation, and pain modulation. These diverse functions of DPP3 are attributed to the degradation of bioactive peptides like angiotensin II. However, because of limitations in currently available assays for determination of active DPP3 in plasma, the exact physiological function of DPP3 and its role in the catabolism of bioactive peptides is understudied.
View Article and Find Full Text PDFBackground: The peptide hormone relaxin-2 is implicated in diverse physiological and pathophysiological processes. Several assays are available for quantification of human relaxin-2, but because stability of the mature peptide in serum is limited, measurement of the more stable connecting peptide (pro-RLX2) might be beneficial.
Methods: Pro-RLX2 was measured in a sandwich immunoluminometric assay using 2 monoclonal antibodies.
Temperate bacteriophages possess a genetic switch which regulates the lytic and lysogenic cycle. The genomes of the enterobacterial telomere phages N15, PY54 and ϕKO2 harbor a primary immunity region (immB) comprising genes for the prophage repressor, the lytic repressor and a putative antiterminator, similar to CI, Cro and Q of lambda, respectively. Moreover, N15 and ϕKO2 contain 3 related operator (OR) sites between cI and cro, while only one site (OR3) has been detected in PY54.
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