Comparison of blood carbonic anhydrase activity of athletes performing interval and continuous running exercise at high altitude

Abstract

The effects of high-intensity interval and continuous exercise on erythrocytes carbonic anhydrase (CA, EC 4.2.1.1) activity levels were scarcely investigated up until now. Here we present a study focused on the CA activity from erythrocytes of athletes experiencing interval and continuous training for 6 weeks, during cold weather and at high altitude (> 1600 m). We observed a 50% increase in the blood CA activity at the second week after initiation of the training in both interval and continuos running groups, whereas the control group did not experience any variation in the enzyme activity levels. In the trained individuals a mild decrease in their body mass, BMI and an increased were also observed. The CA activity returned at the basal values after 4–6 weeks after the training started, probably proving that a metabolic compensation occurred without the need of an enhanced enzyme activity. The unexpected 50% rise of activity for an enzyme which acts as a very efficient catalyst for CO2 hydration/bicarbonate dehydration, such as the blood CA, deserves further investigations for better understanding the physiologic basis of this phenomenon.

Protein Composition of Circulating Extracellular Vesicles Immediately Changed by Particular Short Time of High-Intensity Interval Training Exercise

“…Intensive muscular exercise induces the formation of lactate and CO 2 , which leads to intracellular acidosis. A previous study reported increased blood CA activity 2 weeks after starting interval training ( Tas et al, 2019 ). Therefore, the prompt elevation of CA-1 in EVs may be an adaptive reaction to correct for an acid–base imbalance brought on by HIIT-Ex.…”

Synthesis and Biological Evaluation of Novel Bischalcone Derivatives as Carbonic Anhydrase Inhibitors

“…Enzyme activity was determined spectrophotometrically by following the change in absorbance at 348 nm of 4‐nitrophenylacetate to 4‐nitrophenol over a period of 3 min at 25°C . The enzymatic reaction contained 1.4 mL 0.05 M Tris‐SO 4 buffer (pH 7.4), 1 mL 3 mM 4‐nitrophenylacetate, 0.5 mL H 2 O, and 0.1 mL enzyme solution, in a total volume of 3.0 mL . Inhibitory effects of compounds 3 – 14 were compared with AZA.…”

“…An Activity % − [Inhibitor] graph was drawn for each inhibitor . The curve‐fitting algorithm allowed for obtaining the IC 50 values, working at the lowest concentration of substrate of 0.15 mM, from which K I values were calculated . The catalytic activity of these enzymes was calculated from Lineweaver–Burk plots, as reported previously , and represent the mean from at least three different determinations.…”

Synthesis, in vitroandin silicoBiological Studies of Sulfonamide Chalcones as Esterase Inhibitors

“…[42] The CA I and II enzymatic reaction contained 1.4 mL 0.05 M Tris-SO 4 buffer (pH 7.4), 1 mL 3 mM 4-nitrophenylacetate, 0.5 mL H 2 O and 0.1 mL enzyme solution, in a total volume of 3.0 mL. [43][44][45][46] Inhibitory effects of compounds were compared with AZA. Different inhibitor concentrations were used and all compounds were tested in triplicate at each concentration used.…”