[Implementation of the prevention program in the school dentistry system in the context of healthcare modernization].

The Aim Of The Study: The aim of the study was to develop and implement a program for the prevention of dental diseases for school-age children based on an individual approach to treatment and preventive measures.

Material And Methods: 1848 children aged from 6 to 17 were examined. The main observation group consisted of children from school No.

Superoxide Dismutase 1 Nanozyme for Treatment of Eye Inflammation.

Use of antioxidants to mitigate oxidative stress during ocular inflammatory diseases has shown therapeutic potential. This work examines a nanoscale therapeutic modality for the eye on the base of antioxidant enzyme, superoxide dismutase 1 (SOD1), termed "nanozyme." The nanozyme is produced by electrostatic coupling of the SOD1 with a cationic block copolymer, poly(L-lysine)-poly(ethyleneglycol), followed by covalent cross-linking of the complexes with 3,3'-dithiobis(sulfosuccinimidylpropionate) sodium salt.

Intimate partner violence and ways of coping with stress: cross-sectional survey of female patients in Russian general practice.

Background: Despite World Health Organization guidelines on health service responses to intimate partner violence (IPV) against women general practitioners (GPs) often overlook the problem. Training on IPV addresses GPs' barriers to asking women patients about abuse and responding appropriately. One of the barriers is stereotype of women as passive victims.

Clinical effects of anxiolytic preparation tenoten in complex therapy of essential hypertension.

Addition of modern daily anxiolytic tenoten to complex therapy of patients with arterial hypertension improves the efficiency of treatment and reduces anxiety, which accelerates the development of hypotensive effect. Tenoten can be recommended for the treatment of anxiety symptoms in patients with arterial hypertension.

Epitope-dependent blocking of the angiotensin-converting enzyme dimerization by monoclonal antibodies to the N-terminal domain of ACE: possible link of ACE dimerization and shedding from the cell surface.

In a biomembrane modeling system, reverse micelles, somatic ACE forms dimers via carbohydrate-mediated interaction, providing evidence for the existence of a carbohydrate-recognizing domain on the ACE molecule. We localized this putative region on the N-domain of ACE using monoclonal antibodies (mAbs) to seven different epitopes of ACE. Two mAbs, 9B9 and 3G8, directed to distinct, but overlapping, epitopes of the N-domain of ACE shielded the CRD.

Characterization of bovine atrial angiotensin-converting enzyme.

Bovine atrial angiotensin-converting enzyme (ACE) was purified to electrophoretic homogeneity. The purification procedure included ion-exchange chromatography on DEAE-Toyopearl 650M, affinity chromatography on lisinopril-agarose and gel filtration on Sephadex G-100. The bovine atrial ACE exhibited similar sensitivities to inhibition by lisinopril and captopril as lung ACE (the Ki values for the atrial and lung enzymes differed insignificantly).

Isolation and characterization of the N-domain of bovine angiotensin-converting enzyme.

A method for preparation of a catalytically active fragment of bovine lung angiotensin-converting enzyme (ACE) has been developed. It includes limited proteolysis of the full-length somatic form of the enzyme by trypsin. The resulting fragment corresponds to the N-terminal domain of angiotensin-converting enzyme.

Inhibitor analysis of angiotensin I-converting and kinin-degrading activities of bovine lung and testicular angiotensin-converting enzyme.

Inhibition of bovine lung and testicular angiotensin-converting enzyme (ACE) by some well-known ACE inhibitors (lisinopril, captopril, enalapril), new substances (Nalpha-carboxyalkyl dipeptides PP-09, PP-35, and PP-36), and phosphoramidon was investigated using Cbz-Phe-His-Leu and FA-Phe-Phe-Arg (C-terminal analogs of angiotensin I and bradykinin, respectively) as the substrates. The somatic (two domains) and testicular (single domain) isoenzymes demonstrated different kinetic parameters for hydrolysis of these substrates. All of the inhibitors were competitive inhibitors of both ACE isoforms, and the Ki values were substrate-independent.

Structural organization of membrane and soluble forms of somatic angiotensin-converting enzyme.

The catalytic activity and quaternary structure of soluble (s) and membrane (m) forms of angiotensin-converting enzyme (ACE) were studied in reversed micelles of ternary system Aerosol OT--water--octane. The profile of the dependence of the catalytic activity of the two enzyme forms on the degree of surfactant hydration (micellar size) had several optima corresponding to the function of various active oligomeric enzyme forms; the curves for the s- and m-forms of ACE were different. Data of sedimentation analysis prove that in reversed micelles, s-ACE can exist as monomers, dimers, or tetramers depending on the hydration degree, and the m-form is present as dimers and tetramers only.

Carbohydrates regulate the dimerization of angiotensin-converting enzyme.

Regulation of the catalytic activity and supramolecular structure of angiotensin-converting enzyme was studied in reverse micelles of Aerosol OT in octane as biomembrane model. The kinetic experiments and the sedimentation analysis demonstrated that the enzyme can function both in monomeric and dimeric form. The degree of dimerization was strongly dependent on the concentration and structure of mono- and disaccharides added to the media, indicating the specific role of carbohydrates in forming the supramolecular structure of angiotensin-converting enzyme.

Specific binding of sso II DNA methyltransferase to its promoter region provides the regulation of sso II restriction-modification gene expression.

The regulation of the Sso II restriction-modification system from Shigella sonnei was studied in vivo and in vitro . In lacZ fusion experiments, Sso II methyltransferase (M. Sso II) was found to repress its own synthesis but stimulate expression of the cognate restriction endonuclease (ENase).

Purification of soluble and membrane forms of somatic angiotensin-converting enzyme by cascade affinity chromatography.

Soluble and membrane forms of angiotensin-converting enzyme were purified by cascade affinity chromatography. The enzyme forms were completely separated from each other using their different affinity to the hydrophobic matrix phenyl-silochrome. The enzymes was further purified on affinity sorbent prepared by immobilization of the enzyme inhibitor N-[1(S)-carboxy-5-aminopentyl]glycylphenylalanine on agarose.

Cross-linking of SsoII restriction endonuclease to cognate and non-cognate DNAs.

Specific and non-specific interactions of SsoII restriction endonuclease (R.SsoII) were probed by the method of covalent attachment to modified DNA containing an active monosubstituted pyrophosphate internucleotide bond instead of a phosphodiester one. R.

The interaction of DNA duplexes containing 2-aminopurine with restriction endonucleases EcoRII and SsoII.

Oligonucleotides containing 2-aminopurine (2-AP) in place of G or A in the recognition site of EcoRII (CCT/AGG) or SsoII (CCNGG) restriction endonucleases have been synthesized in order to investigate the specific interaction of DNA with these enzymes. Physicochemical properties (CD spectra and melting behaviour) have shown that DNA duplexes containing 2-aminopurine exist largely in a stable B-like form. 2-Aminopurine base paired with cytidine, however, essentially influences the helix structure.

The SsoII and NlaX DNA methyltransferases: overproduction and functional analysis.

Overproduction of the NlaX DNA methyltransferase (M.NlaX) in an Escherichia coli host conferred resistance to SsoII restriction endonuclease (R.SsoII) digestion.

Interaction of the MvaI and SsoII methyltransferases with DNAs altered at the central base pair of the recognition sequence.

The interaction of the MvaI and SsoII DNA methyltransferases (MTases; M.MVaI and M.SsoII, respectively) with a set of synthetic DNA duplexes, containing a M.

Analysis of the nucleotide and derived amino acid sequences of the SsoII restriction endonuclease and methyltransferase.

A 2648-bp fragment from the P4 plasmid of Shigella sonnei strain 47 coding for the SsoII restriction endonuclease (ENase) and methyltransferase (MTase) (recognition sequence 5'-CCNGG) was sequenced. Two divergently arranged open reading frames of 905 bp for the SsoII ENase (R.SsoII) and 1137 bp for the MTase (M.

Cleavage of synthetic substrates containing non-nucleotide inserts by restriction endonucleases. Change in the cleavage specificity of endonuclease SsoII.

A study was made of the interaction between restriction endonucleases recognizing CCNGG (SsoII and ScrFI) or CCA/TGG (MvaI and EcoRII) DNA sequences and a set of synthetic substrates containing 1,3-propanediol, 1,2-dideoxy-D-ribofuranose or 9-[1'-hydroxy-2'-(hydroxymethyl)ethoxy] methylguanine (gIG) residues replacing either one of the central nucleosides or dG residues in the recognition site. The non-nucleotide inserts (except for gIG) introduced into the recognition site both increase the efficiency of SsoII and change its specificity. A cleavage at the noncanonical position takes place, in some cases in addition to the correct ones.

Characterization of the genetic determinants of SsoII-restriction endonuclease and modification methyltransferase.

The genes encoding SsoI and SsoII restriction endonuclease (ENase) and methyltransferase (MTase) are located on the small plasmids P6 and P4, respectively, of Shigella sonnei strain 47. Functions provided by plasmids P5, P7 and P9, which include colicinogenicity and immunity to colicin E1, resistance to streptomycin (Sm), and conjugative DNA transfer, respectively, have also been identified. The genes of the SsoII restriction-modification (R-M) system have been cloned into Escherichia coli expressing the 35-kDa (ENase) and 43-kDa (MTase) products.

Factors of activation and stabilization of DNA-methylases from Shigella sonnei 47 and Mycobacterium smegmatis butyricum cells.

A comparative study of factors of activation and stabilization of individual DNA-methylases from two bacterial strains--Shigella sonnei 47 and Mycobacterium smegmatis butyricum--isolated by isoelectrofocusing in a pH gradient has been carried out. Storage of enzymes at +4 degrees C (pH 7.5) is accompanied by periodic changes in the methylating activity.

Sequence specificity of isolated DNA-adenine methylases from Mycobacterium smegmatis (butyricum) and Shigella sonnei 47 cells.

A set of four individual DNA-adenine methylases differing in pI (isoelectric point) values (MMbu4.2, MMbu6.4, MMbu7.

Sequence specificity of isolated DNA-cytosine methylases from Shigella sonnei 47 cells.

Five individual DNA-cytosine methylases differing in pI (isoelectric point) values are present in Shigella sonnei 47-cells. The sequence specificity of each of those was determined 'in vitro' by a highly efficient combined approach that included pyrimidine tract (isostic) analysis, identification of the immediate neighbourhood of the methylated base within the recognition sequence and the calculation method. The enzyme with pI 5.

Isoelectric focusing of bacterial DNA methylases.

The multiplicity of bacterial DNA methylases has been shown for new microorganisms, Mycobacteria and Shigella, by a double-step procedure including column chromatography followed by isoelectric focusing of the total methylase fraction. The profiles of the DNA methylating activity of Sh. sonnei 47 and M.

DNA-methylating activity of mycobacteria.

The methylating activity of the four mycobacterium strains Mycobacterium phlei, Mycobacterium smegmatis strain Butyricum, Mycobacterium smegmatis strain Rabinowitz, lysogenic Mycobacterium smegmatis strain Rabinowitz was studied in vitro. All the four strains were found to have methylating activity; enzyme containing extracts of M. smegmatis strain Butyricum and M.