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The content of superoxide dismutase (SOD) and catalase (CAT) isoenzymes in reproductive organs and freshly obtained ejaculates of wild boars were studied. It was established that there were five SOD isoenzymes (S1 – S5) in the tissues of the reproductive organs and spermatozoa of the appendages and freshly obtained ejaculates of wild boars. At the same time, in the investigated tissues, features of the isoenzyme composition were established, which were manifested by a different percentage of enzyme proteins in their total content. In particular, testis tissue were characterized by the maximum content of S3 (46.5 ± 2.4%). In the tissue of the appendages, compared to the testes, the ratio of isoenzymes changes in the direction of a decrease in the content of S3 and an increase in S2. The difference between these proteins was, respectively, 11.8 and 13.1% (P < 0.05). In the tissue of appendages, content of S2 isoenzyme increased from 33.2 ± 2.7% in the head to 6.2% in the body and 14.6% in the tail. When the part of the appendage changed from the head to the body, the content of S5 and S1 SOD isoenzymes decreased, respectively, from 6.3 ± 0.1 and 16.1 ± 1.2% to 1.3 (Р < 0.01) and 4,1% (P < 0.05). The SOD protein content in epididymal sperm differed from tissue. In spermatozoa from the head of the appendages, the maximum content was of S2 (37.4 ± 2.8%), lower by 12.9 and 17.3%, respectively, than S3 and S1, by 22.5% less than S4 and the least (3.1 ± 0.2%) of S5-isoenzymes. The advancement of spermatozoa from the head to the body and tail of the appendages was characterized by an increase in the content of S3- and S2-isoenzymes, respectively, by 2.1–9.9% (P < 0.05) and 1.4–7.7%. At the same time, the content of S1 decreases by 3.9–12.7% (Р < 0.001), while the content of S5- and S4-isoenzymes did not change and is within the limits of, respectively, 2.7-3.1% and 14.3- 15.4%. The SOD isoenzyme spectrum of boar ejaculates was characterized by a high content of S5 (43.9 ± 3.55%) and S4 (30.9 ± 3.17%) isoenzymes, compared to the content of enzyme isoenzymes in reproductive organs and epididymal sperm. Among the cytoplasmic proteins of SOD, S2 was in the largest quantity – 15.5 ± 3.92%, and the content of S3 and S1 was lower by 10.4 and 11.1%, respectively. In reproductive tissues, as well as in spermatozoa from the head of the epididymis, two catalase isoenzymes - CAT1 and CAT2 - were detected. CAT2 was not detected in the tissues of the body and tail of the appendages and spermatozoa obtained from the indicated parts. The content of CAT with a change in the morphological part of the appendix decreased in the tissue of the body and tail by 18.3 (Р < 0.01) and 29.2% (Р < 0.001), respectively, compared to the head of the epididymis. Similarly, the content of CAT decreased in sperm when passing from the head to the body and tail of the appendages, respectively, by 21.4 (Р < 0.01) and 29.5% (Р < 0.001). The presence of two catalytically active proteins of the enzyme CAT1 (20.4 ± 5.78%) and CAT2 (79.6 ± 5.78%) were established in boar ejaculates. The values of SOD and CAT protein content in ejaculates depended on their physiological characteristics and individual characteristics of boars and are manifested by different content of the same isoenzyme.
The content of superoxide dismutase (SOD) and catalase (CAT) isoenzymes in reproductive organs and freshly obtained ejaculates of wild boars were studied. It was established that there were five SOD isoenzymes (S1 – S5) in the tissues of the reproductive organs and spermatozoa of the appendages and freshly obtained ejaculates of wild boars. At the same time, in the investigated tissues, features of the isoenzyme composition were established, which were manifested by a different percentage of enzyme proteins in their total content. In particular, testis tissue were characterized by the maximum content of S3 (46.5 ± 2.4%). In the tissue of the appendages, compared to the testes, the ratio of isoenzymes changes in the direction of a decrease in the content of S3 and an increase in S2. The difference between these proteins was, respectively, 11.8 and 13.1% (P < 0.05). In the tissue of appendages, content of S2 isoenzyme increased from 33.2 ± 2.7% in the head to 6.2% in the body and 14.6% in the tail. When the part of the appendage changed from the head to the body, the content of S5 and S1 SOD isoenzymes decreased, respectively, from 6.3 ± 0.1 and 16.1 ± 1.2% to 1.3 (Р < 0.01) and 4,1% (P < 0.05). The SOD protein content in epididymal sperm differed from tissue. In spermatozoa from the head of the appendages, the maximum content was of S2 (37.4 ± 2.8%), lower by 12.9 and 17.3%, respectively, than S3 and S1, by 22.5% less than S4 and the least (3.1 ± 0.2%) of S5-isoenzymes. The advancement of spermatozoa from the head to the body and tail of the appendages was characterized by an increase in the content of S3- and S2-isoenzymes, respectively, by 2.1–9.9% (P < 0.05) and 1.4–7.7%. At the same time, the content of S1 decreases by 3.9–12.7% (Р < 0.001), while the content of S5- and S4-isoenzymes did not change and is within the limits of, respectively, 2.7-3.1% and 14.3- 15.4%. The SOD isoenzyme spectrum of boar ejaculates was characterized by a high content of S5 (43.9 ± 3.55%) and S4 (30.9 ± 3.17%) isoenzymes, compared to the content of enzyme isoenzymes in reproductive organs and epididymal sperm. Among the cytoplasmic proteins of SOD, S2 was in the largest quantity – 15.5 ± 3.92%, and the content of S3 and S1 was lower by 10.4 and 11.1%, respectively. In reproductive tissues, as well as in spermatozoa from the head of the epididymis, two catalase isoenzymes - CAT1 and CAT2 - were detected. CAT2 was not detected in the tissues of the body and tail of the appendages and spermatozoa obtained from the indicated parts. The content of CAT with a change in the morphological part of the appendix decreased in the tissue of the body and tail by 18.3 (Р < 0.01) and 29.2% (Р < 0.001), respectively, compared to the head of the epididymis. Similarly, the content of CAT decreased in sperm when passing from the head to the body and tail of the appendages, respectively, by 21.4 (Р < 0.01) and 29.5% (Р < 0.001). The presence of two catalytically active proteins of the enzyme CAT1 (20.4 ± 5.78%) and CAT2 (79.6 ± 5.78%) were established in boar ejaculates. The values of SOD and CAT protein content in ejaculates depended on their physiological characteristics and individual characteristics of boars and are manifested by different content of the same isoenzyme.
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