The enzyme activity dynamic relationship with the content of structural polypeptides of enterocyte membranes in cattle fetal
The article performs new data on the relationship between the hydrolytic and transport enzyme activity at different poles of the enterocytes plasmolemma of cow's fetal large intestine with the content of individual fractions of polypeptides. An expressive direct dependence of enzyme activity dynamics on the apical and basolateral membranes of enterocytes containing low molecular weight proteins and an inverse relationship with the concentration of proteins with medium and large molecular weights has been proved. It was found that the alkaline activity of the phosphatase and γ-glutamyltransferase on the apical domain of enterocyte plasmolemma is directly related to the proteins content with molecular masses of 9.6–14.2 kD, 21 kD, 22.5 kD, 26 kD, 33 kD, 35 kD, 170–185 kD, and 205 kD (P ≤ 0.05–0.001). Gamma-glutamyltransferase activity is straightly related to protein quantity with molecular weights of 15.5 kDa and 39 kD (P ≤ 0.05). In contrast, alkaline phosphatase and GGT activity have inverse correlations with the content of polypeptides with molecular masses of 46 kD, 63 kD, and 250 kD in the apical membrane of enterocytes (P ≤ 0.01–0.001). The lactase activity in the cattle enterocytes apical membrane during the test period has significant direct correlations only with the amount of the polypeptide of polypeptides with molecular weights of 31 kD, 39 kD, and 100 kD (P ≤ 0.05–0.01) and inverse relationships containing proteins with molecular masses of 46 kD and 120 kD (P ≤ 0.05). A linear dependence of the different ATPase activity of the apical membrane of red blood cells containing proteins with molecular weights of 9.6–14.2 kD, 15.5 kD, 21 kD, 22.5 kD, 33 kD, 35 kD, 39 kD, and 205 kD (P ≤ 0.05–0.001) was observed. Alkaline phosphatase activity in the apical membrane of enterocytes is only directly related to the number of proteins with molecular weights of 17 kD and 24 kD (P ≤ 0.001) in this domain. It inversely depends on the content of proteins with molecular masses of 9.6–14.2 kD and 52 kD (P ≤ 0.001). G-glutamyltransferase activity is inversely related to protein content with molecular weights of 43 kD, 52 kD, 66 kD, 87 kD, and 100 kD and 155 kD (P ≤ 0.001). The Ca2+, Mg2+-ATPase of the basolateral membrane activity of enterocytes is directly related to the protein amount with molecular weights of 26 kD (P ≤ 0.01), Mg2+-ATPase and Mg2+-ATPase with protein content with the molecular value of 100 kD (P ≤ 0.05).
Filho, N., Carlos, L. et al. (2016). Use of the enzyme gamma–glutamyl transferase (GGT) as an indirect measure of passive transfer of immunity in holstein calves and association with the occurrence of diarrhea after birth. Bioscience Journal, 32(1), 455–459. doi: 10.14393/BJ-v32n2a2016-29476.
Havrylin, P. M., & Masiuk, D. M. (2004). Zakonomirnosti mor-fohenezu tkanynnykh komponentiv orhaniv krovotvorennia ta imunnoho zakhystu u teliat. Naukovyi visnyk Lvivskoho natsion-alnoho universytetu veterynarnoi medytsyny ta biotekhnolohii im. S. Z. Gzhytskoho. Seriia: Veterynarna medytsyna, 6(1), 16–25 (in Ukrainian).
Masiuk, D. M. (2020). Interconnection between the expression of fc-γ-receptor proteins and the activity of enzymes in the empty intestine plasmolema of the empty intestine of the great horny skin. Ukrainian Chasopis of Veterinary Sciences, 11(1), 70–80.
Panizza, E., Zhang, L., Fontana, J. M., Hamada, K. et al. (2019). Ouabain Regulated Phosphoproteome Reveals Molecular Mech-anisms Behind Na, K–ATPase Control of Cell Adhesion, Prolif-eration and Survival. The FASEB Journal, 33(9), 10193–10206. doi: 10.1096/fj.201900445R.
Saakes, M., Hamelers, H. V. M., & Van Egmond, W. J. (2018). Method for Operating of a Regenerative Bipolar Membrane Fuel Cell, and Regenerative Bipolar Membrane Fuel Cell There. 15556887.
St Johnston, D. I., & Sanson, B. (2011). Epithelial polarity and morphogenesis. Curr Opin Cell Biol., 23(5), 540–546. doi: 10.1016/j.ceb.2011.07.005.
Tarabova, L., Makova Z., Piesova, E., Szaboova, R., & Faixova, Z. (2016). Intestinal mucus layer and mucins (a review). Folia Vet-erinaria, 60(1), 21–25. doi: 10.1515/fv-2016-0003.
Tilney, L. G., Hatano, S., Ishikawa, H., & Mooseker, M. S. (1973). The polymerization of actin: its role in the generation of the acro-somal process of certain echinoderm sperm. J. Cell Biol, 59(1), 109–126. doi: 10.1083/jcb.59.1.109.
Valadão, L., Da Silva, H. M., & Da Silva, F. M. (2018). Bovine Embryonic Development to Implantation. Embryogenesis. IntechOpen. doi: 10.5772/intechopen.80655.