Tag Archives: acid phosphatase

Changes in the activity of phosphatases, calcium and phosphorus in rats with the different courses of gingivitis under correction by anti-inflammatory gel

O. Avdeev1, R. Drevnitska2, N. Gevkaliuk1,
Yu. Bandrivsky1*, A. Boykiv3

1Department of Pediatric Dentistry, I. Horbachevsky Ternopil National
Medical University, Ternopil, Ukraine;
2Department of Dental Therapy, I. Horbachevsky Ternopil National
Medical University, Ternopil, Ukraine;
3Department of Orthopedic Dentistry, I. Horbachevsky Ternopil National
Medical University, Ternopil, Ukraine;
*e-mail: bandrivsky@tdmu.edu.ua

Received: 27 January 2022; Revised: 20 March 2022;
Accepted: 14 October 2022; Available on-line: 19 December 2022

The aim of the study was to evaluate changes in the activity of acid and alkaline phosphatases, calcium and phosphorus levels in rats with different courses of experimental gingivitis upon treatment with anti-inflammatory gel with Neovitin and peptide complexes. The experiment was conducted on 100 white nonlinear male rats aged 5-6 months divided into 10 groups: 1 control and 9 – with different courseі of gingivitis. The activity of alkaline and acid phosphatase (ALP, ACP), the levels of calcium (Ca) and phosphorus (P) in rat blood serum and gingiva supernatant were determined. It was found that upon gingivitis, the activity of ALP in blood serum decreased and in gingiva supernatant increased in all groups of animals compared to the control group. The activity of ACP in the serum decreased in hypoergic and hyperergic animal groups and increased in normergia, and in gingiva supernatant increased in all groups: by 2 times in normoergic and hypoergic animals and by 1.4 times in hyperergic. The treatment with anti-inflammatory gel normalized the activity of ALP in both serum and supernatant and decreased the ACP activity in the serum of animals in hypo- and hyperergic groups. The content of serum Ca increased in all groups, and in the supernatant of the gingiva even exceeded the control value. The content of phosphorus in the supernatant of periodontal tissues decreased. The development of the inflammatory process in the periodontium of rats with gingivitis was accompanied by changes in the activity of ACP, ALP, the content of Ca and P in the blood serum and gingival supernatant. The treatment with gel containing neovitin and peptide complexes had a more pronounced therapeutic effect in rats with unchanged reactivity of the organism.

Identification of thiamine monophosphate hydrolyzing enzymes in chicken liver

I. K. Kolas, A. F. Makarchikov

Grodno State Agrarian University;
Institute of Biochemistry of Biologically Active Compounds,
National Academy of Sciences of Belarus, Grodno;
e-mail: a_makarchikov@yahoo.com

In animals, thiamine monophosphate (TMP) is an intermediate on the path of thiamine diphosphate, the coenzyme form of vitamin B1, degradation. The enzymes involved in TMP metabolism in animal tissues are not identified hitherto. The aim of this work was to study TMP hydrolysis in chicken liver. Two phosphatases have been found to contribute to TMP hydrolysis in liver homogenate. The first one, possessing a maximal activity at pH 6.0, is soluble, whereas the second one represents a membrane-bound enzyme with a pH optimum of 9.0. Membrane-bound TMPase activity was enhanced 1.7-fold by 5 mM Mg2+ ions and strongly inhibited by levami­sole in uncompetitive manner with Ki of 53 μM, indicating the involvement of alkaline phosphatase. An apparent Km of alkaline phosphatase for TMP was calculated from the Hanes plot to be 0.6 mM. The soluble TMPase has an apparent­ Km of 0.7 mM; this enzyme is Mg2+ independent and insensitive to levamisole. As estimated by gel filtration on a Toyopearl HW-55 column, the soluble enzyme has a molecular mass of 17.8 kDa, TMPase activity being eluted simultaneously with peaks of flavinmononucleotide and p-nitrophenyl phosphatase activity. Thus, TMP appears to be a physiological substrate for a low-molecular weight acid phosphatase, also known as low-molecu­lar-weight protein phosphotyrosine phosphatase.