Effect of Acute Hypoxia and Hydrogen Sulfide Contamination on the Succinate Dehydrogenase Activity and Adenylate Complex of Tissues in the Bivalve Mollusk Anadara kagoshimensis (Tokunaga, 1906)

Мұқаба

Дәйексөз келтіру

Толық мәтін

Ашық рұқсат Ашық рұқсат
Рұқсат жабық Рұқсат берілді
Рұқсат жабық Тек жазылушылар үшін

Аннотация

The separate effects of acute hypoxia and hydrogen sulfide load on the marker enzyme succinate dehydrogenase (SDH) of the mitochondrial respiratory chain and the adenylate status of tissues in the bivalve mollusk Anadara kagoshimensis (Tokunaga, 1906), a species tolerant to these groups of factors, were studied under experimental conditions. The study was carried out on adult individuals with a shell height of 23–34 cm. The control group of bivalves was kept in the water with an oxygen concentration of 7.0–8.2 mgО2/L. One experimental group was exposed to acute hypoxia (0.1 mgО2/L) and another to hydrogen sulfide load (6 mgS2–/L). The exposure period in both cases was 48 h. The water temperature was maintained at 17–20°C. The acute hypoxia led to an increase in the SDH activity in all the studied tissues (gills, foot, and hepatopancreas). This reaction was not observed under the hydrogen sulfide load. The energy state of the tissues decreased in both cases. This was expressed as a decrease in the ATP and ADP content accompanied by an increase in the AMP content, which allows implementation of the adenylate kinase reaction. These changes were more pronounced in the presence of hydrogen sulfide. However, the adenylate pool and adenylate energy charge (AEC) values remained at a relatively high level, which indicates the ability of ark clam to exist in the near-bottom water layers with a low level of oxygen and the presence of hydrogen sulfide. It is assumed that ark clam’s mitochondria have an alternative oxidase that is not sensitive to the presence of sulfides in water.

Толық мәтін

Рұқсат жабық

Авторлар туралы

A. Soldatov

Kovalevsky Institute of Biology of the Southern Seas, Russian Academy of Sciences; Sevastopol State University

Хат алмасуға жауапты Автор.
Email: alekssoldatov@yandex.ru
ORCID iD: 0000-0002-9862-123X
Ресей, Sevastopol; Sevastopol

Yu. Bogdanovich

Kovalevsky Institute of Biology of the Southern Seas, Russian Academy of Sciences

Email: alekssoldatov@yandex.ru
ORCID iD: 0000-0002-8239-4968
Ресей, Sevastopol

N. Shalagina

Kovalevsky Institute of Biology of the Southern Seas, Russian Academy of Sciences

Email: alekssoldatov@yandex.ru
ORCID iD: 0000-0001-6195-6135
Ресей, Sevastopol

V. Rychkova

Kovalevsky Institute of Biology of the Southern Seas, Russian Academy of Sciences

Email: alekssoldatov@yandex.ru
ORCID iD: 0000-0003-3797-715X
Ресей, Sevastopol

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2. Fig. 1. Succinate dehydrogenase (SDH) activity in anadara tissues (1 – normoxia; 2 – acute hypoxia; 3 – hydrogen sulfide load; *p< 0.05 relative to control; *p< 0.05 relative to control; n = 9).

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3. Fig. 2. Pool of adenylates in anadara tissues (1 – normoxia; 2 – acute hypoxia; 3 – hydrogen sulfide load; n = 9).

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4. Fig. 3. Content of individual fractions of adenylates (ATP, ADP, AMP) in anadara tissues (1 – normoxia; 2 – acute hypoxia; 3 – hydrogen sulfide load; *p< 0.05 relative to control; n = 9).

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5. Fig. 4. Adenylate energy charge (AEC) in anadara tissues (1 – normoxia; 2 – acute hypoxia; 3 – hydrogen sulfide load; *p< 0.05 relative to control; n = 9).

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