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    Wyświetlanie 1-2 z 2
    Tytuł:
    Acrosin system of dog spermatozoa and reproductive tract secretions
    Autorzy:
    Strzezek, R
    Koziorowska-Gilun, M.
    Filipowicz, K.
    Powiązania:
    https://bibliotekanauki.pl/articles/32251.pdf
    Data publikacji:
    2010
    Wydawca:
    Polska Akademia Nauk. Czytelnia Czasopism PAN
    Tematy:
    dog
    semen
    proacrosin
    acrosin
    spermatozoon
    sperm-rich fraction
    whole ejaculate
    antitrypsin activity
    antitrypsin inhibitor
    seminal plasma
    ejaculate
    Beagle dog
    mixed breed
    Opis:
    The aim of this study was to determine the activity of proacrosin and acrosin in spermatozoa originating from the sperm-rich fractions (SRF) and whole ejaculates (WE) of dog semen. In addition, experiments were conducted to determine the activity of antitrypsin inhibitors in the fluids of different ejaculate fractions and whole seminal plasma. Ejaculates were collected from five dogs of mixed breed and one Beagle dog (aged from 2 to 9 years). In the SRF, it was confirmed that the activity of the free acrosin form was predominant (acrosin / proacrosin; 2.38 ± 0.22 / 1.05 ± 0.08 mIU / 106 spermatozoa). On the other hand, spermatozoa originating from the WE exhibited significantly higher (p<0.05) proacrosin activity (proacrosin / acrosin; 2.19 ± 0.19 /1.30 ± 0.11 mIU / 106 spermatozoa). Furthermore, acrosin inhibitor activity was lower in the fluids of the pre-sperm fraction (0.09 ± 0.006 IU / cm3), whereas it was higher in the fluids of the post-sperm fraction (0.11 ± 0.007 IU / cm3). Using PAGE analysis, the antitrypsin activity of the enzyme was represented by the presence of one electrophoretic band in the fluids of the pre-sperm and post-sperm fractions and whole seminal plasma. Furthermore, two electrophoretic bands were detected in the fluids of the SRF. The findings of this study indicate that specific proteinase inhibitors present in the individual ejaculate fractions of dog semen may act by stabilizing the sperm acrosin system.
    Źródło:
    Polish Journal of Veterinary Sciences; 2010, 13, 1; 69-73
    1505-1773
    Pojawia się w:
    Polish Journal of Veterinary Sciences
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Applicability of 2,4-dinitrophenylhydrazine (DNPH) method of protein oxidative damage measurement in the seminal plasma of canine (Canis lupus familiaris) and stallion (Equus caballus)
    Autorzy:
    Mogielnicka-Brzozowska, M.
    Woźniak, M.J.
    Cichowska, A.W.
    Fraser, L.
    Kraziński, B.
    Strzezek, R.
    Zielińska, D.
    Powiązania:
    https://bibliotekanauki.pl/articles/16647556.pdf
    Data publikacji:
    2023
    Wydawca:
    Polska Akademia Nauk. Czasopisma i Monografie PAN
    Tematy:
    2,4-dinitrophenylhydrazine
    canine
    protein carbonylation
    seminal plasma
    stallion
    Opis:
    Seminal plasma (SP) proteins are responsible for sperm functional quality. Developing a reliable method to determine the degree of oxidative damage of these proteins is important for establishing semen fertilizing ability. The main aim of the study was to verify the applicability of protein carbonyl derivatives measurement in the SP of canine and stallion, using a method with 2,4-dinitrophenylhydrazine (DNPH). The research material consisted of ejaculates obtained from eight English Springer Spaniels, and from seven half-blood stallions during the breeding and non-breeding season. The content of carbonyl groups in the SP was measured on the basis of the reactions with DNPH. The following reagent variants were used to dissolve protein precipitates: Variant 1 (V1) – 6M Guanidine solution and Variant 2 (V2) – 0.1M NaOH solution. It has been shown that to obtain reliable results for the measurement of protein carbonylated groups in the dog and horse SP, both 6M Guanidine and 0.1M NaOH may be used. A correlation was also found between the number of carbonyl groups and the total protein content in the canine (V1: r = -0.724; V2: r = -0.847) and stallion (V1: r = -0.336; V2: r = -0.334) SP. Additionally, the study showed a higher content (p≤0.05) of protein carbonyl groups in the stallion SP in the non-breeding season compared to the breeding season. The method based on the reaction with DNPH, due to its simplicity and cost effectiveness, appears to be suitable for large-scale application in the determination of the SP proteins oxidative damage in dog and horse semen.
    Źródło:
    Polish Journal of Veterinary Sciences; 2023, 26, 2; 177-184
    1505-1773
    Pojawia się w:
    Polish Journal of Veterinary Sciences
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-2 z 2

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