Oral peroxidase, one of the most important salivary antioxidant enzymes, is subjected to alternation due to various body conditions. The aim of this study was to assess the effect of exercise intensity on salivary peroxidase activity. Using a randomized design, ten healthy male university students (mean age, 23.22; s (x) = 2.34 years) completed treadmill runs with initial velocity 6.73 km/h at the rate of 1.58 km/h increase every 3 min until exhaustion. Unstimulated whole saliva collected over a 5-min period in pre-weighed tubes before, immediately after exercise, and 1 h after exercise was analyzed for total protein and saliva peroxidase activity. The saliva flow rate ranged from 0.08 to 1.40 ml min(-1) at rest and was not significantly affected by the exercise. Peroxidase activity in each sample was measured using 4-amino antipyrine as substrate. In the incremental exhaustion run and also at 75% VO(2max), the secretion rates of peroxidase increased. No significant changes in saliva flow rate were observed in any treadmill run. Treadmill runs at 75% VO(2max) and to exhaustion increased the activity of peroxidase immediately after exercise which decreased after 1 h. It was concluded that short-duration, high-intensity exercise increases the activity rate of peroxidase despite no change in the saliva flow rate. These effects appear to be associated with changes in sympathetic activity and not the hypothalamic pituitary adrenal axis.

A comparison of the two most famous groups of calcium-regulated photoproteins, cnidarians and ctenophores, showed unexpectedly high degree of structural similarity regardless of their low sequence identity. It was suggested these photoproteins can play an important role in understanding the structural basis of bioluminescence activity. Based on this postulate, in this study the cDNA of mnemiopsin from luminous ctenophore Mnemiopsis leidyi was cloned, expressed, purified and sequenced. The purified cDNA, with 621 base pairs, coded a 206 residues protein. Sequence of mnemiopsin showed 93.5 and 51% similarity to other ctenophore proteins and cnidarians, respectively. The cDNA encoding apo-mnemiopsin of M. leidyi was expressed in Escherichia coli. The purified apo-protein showed a single band on SDS-PAGE (molecular weight ~27 kDa). A semi-synthetic mnemiopsin was prepared using coelenterazine and EDTA and its luminescence activity was measured in the presence of CaCl(2). The results showed an optimum pH of 9.0 and lower calcium sensitivity compared to aequorin. Comparison of amino acid residues in substrate binding site indicated that binding pocket of ctenophores contains less aromatic residues than cnidarians. This can lead to a decline in the number of stacking interactions between substrate and protein which can affect the stability of coelenterazine in binding cavity. Structural comparison of photoproteins with low sequence identity and high 3D structural similarity, can present a new insight into the mechanism of light emission in photoproteins.

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