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1.
Public Health Nurs ; 17(2): 111-20, 2000.
Article in English | MEDLINE | ID: mdl-10760193

ABSTRACT

Few studies of utilization and satisfaction with prenatal care services have been conducted internationally. In this study, utilization and satisfaction with prenatal care services in St. Petersburg, Russia were examined using Aday and Andersen's (1974) A Framework for the Study of Access to Medical Care. This study was conducted under the auspices of the European Region, World Health Organization (WHO) Healthy Cities Project, which promotes a community-based intersectoral approach to meeting health needs. The convenience sample included 397 women with uncomplicated pregnancies and normal deliveries, representing an 86% response rate. Multiple regression and path analysis found significant predictors of prenatal care utilization and satisfaction. They were different, however, from those posited in the theoretical model. This indicates that Aday and Andersen's health care services model is specific to the U. S. health care system, where it originated. The Russian health care system has been and remains different from that of the United States. If the reformed Russian health care system takes on aspects of the U. S. health care system, the utility of Aday and Andersen's theoretical model may change.


Subject(s)
Models, Theoretical , Patient Satisfaction , Prenatal Care/standards , Adolescent , Adult , Cross-Sectional Studies , Demography , Female , Humans , Pregnancy , Prenatal Care/organization & administration , Prenatal Care/statistics & numerical data , Russia
2.
J Nurs Meas ; 8(2): 117-29, 2000.
Article in English | MEDLINE | ID: mdl-11227579

ABSTRACT

Patient satisfaction with health services is used as a measure of the quality of patient care received. The emphasis on accountability and patient as consumer has contributed to the growing interest in studying patient satisfaction. Patient satisfaction with prenatal care services has not been extensively studied including instrumentation to develop a satisfaction scale. The purpose of this study was to develop a reliable and valid scale to measure satisfaction with prenatal care services in St. Petersburg, Russia, using the 6 satisfaction dimensions in Aday and Andersen's Theoretical Framework (1974). It was conducted under the auspices of the World Health Organization, Healthy Cities Project. Although the study was conducted internationally, it provides a basis for further testing of reliability and validity in the United States. A convenience sample of 397 women with uncomplicated pregnancies and normal deliveries was studied (86% response rate). Content, construct, and predictive validity, and reliability testing using Cronbach's alpha was conducted. The scale was found to be an adequate and theoretically sound measure of satisfaction with prenatal care services in Russia. However, rather than the 6 hypothesized satisfaction dimensions, Russian women identified 2 satisfaction subscales or measures for quality of prenatal care received. One was, as hypothesized, convenience, and the other was the doctor's behavior.


Subject(s)
Nursing Research/methods , Patient Satisfaction , Prenatal Care , Surveys and Questionnaires , Adolescent , Adult , Factor Analysis, Statistical , Female , Humans , Pregnancy , Reproducibility of Results , Russia
3.
West J Nurs Res ; 21(3): 372-86, 1999 Jun.
Article in English | MEDLINE | ID: mdl-11512204

ABSTRACT

This study was conducted in St. Petersburg, Russia, under the auspices of the World Health Organization, Healthy Cities Project, and the St. Petersburg Healthy City Project. The purpose of this study was to investigate the predict use of prenatal care services (utilization) and satisfaction with the services. A high maternal mortality rate and low attendance at prenatal clinics brought this health care issue to the forefront of the St. Petersburg Healthy City Project agenda. Aday and Andersen's conceptual model was used to investigate use of and satisfaction with prenatal care services. Several characteristics of pregnant women were found to influence early use of prenatal care services and women's level of satisfaction. Need had no influence in explaining when women started prenatal care or satisfaction with the services. Lastly, there was no relationship between early use of prenatal care services and women's level of satisfaction with the services.


Subject(s)
Ambulatory Care Facilities/statistics & numerical data , Ambulatory Care Facilities/standards , Patient Satisfaction , Pregnancy/psychology , Prenatal Care/statistics & numerical data , Prenatal Care/standards , Adolescent , Adult , Cross-Sectional Studies , Female , Health Services Research , Humans , Maternal Mortality , Models, Psychological , Needs Assessment , Nursing Methodology Research , Predictive Value of Tests , Quality of Health Care , Regression Analysis , Russia/epidemiology , Surveys and Questionnaires , Urban Health/statistics & numerical data
4.
Mol Cell Biochem ; 125(2): 105-14, 1993 Aug 25.
Article in English | MEDLINE | ID: mdl-8283966

ABSTRACT

Subcellular distribution of aminoacyl-tRNA synthetase activities has been studied in normal rabbit liver and under experimental myocardial ischemia (EMI). An increase in the activity of a number of aminoacyl-tRNA synthetases in postmitochondrial and postribosomal supernatants from rabbit liver has been determined 12 hr after EMI. Gel chromatography of the postribosomal supernatant on Sepharose 6B shows that aminoacyl-tRNA synthetase activities are distributed among the fractions with M(r) 1.82 x 10(6), 0.84 x 10(6) (high-M(r) aminoacyl-tRNA synthetase complexes) and 0.12-0.35 x 10(6). In the case of EMI aminoacyl-tRNA synthetase activities are partly redistributed from the 1.82 x 10(6) complex into the 0.84 x 10(6) complex. The catalytic properties of both free and complex leucyl-tRNA synthetases have been compared. KM for all the substrates are the values of the same order in norm and under EMI. A decrease in some aminoacyl-tRNA synthetase activities associated with polyribosomes has been observed 12 hr after EMI. The interaction of aminoacyl-tRNA synthetases with polyribosomes stimulates the catalytic activity of some enzymes and protects them from heat inactivation in vitro. It is assumed that the changes in association of aminoacyl-tRNA synthetases with high-M(r) complexes and compartmentalization of these enzymes on polyribosomes may be related to the alteration of protein biosynthesis under myocardial ischemia.


Subject(s)
Amino Acyl-tRNA Synthetases/metabolism , Liver/enzymology , Myocardial Ischemia/enzymology , Subcellular Fractions/enzymology , Animals , Catalysis , Hot Temperature , Leucine-tRNA Ligase/metabolism , Male , Mitochondria, Liver/enzymology , Rabbits , Ribosomes/enzymology
5.
Biokhimiia ; 57(8): 1123-41, 1992 Aug.
Article in Russian | MEDLINE | ID: mdl-1391218

ABSTRACT

Data on structural and functional peculiarities of eukaryotic aminoacyl-tRNA synthetases (structure, supermolecular organization, and localization in eukaryotic cell) are reviewed. The functional significance of aminoacyl-tRNA synthetase association with high molecular weight complexes and other cellular components is discussed.


Subject(s)
Amino Acyl-tRNA Synthetases/metabolism , Eukaryotic Cells/enzymology , Amino Acyl-tRNA Synthetases/chemistry , Molecular Weight , Structure-Activity Relationship
6.
Patol Fiziol Eksp Ter ; (1): 49-51, 1992.
Article in Russian | MEDLINE | ID: mdl-1625935

ABSTRACT

The authors studied teh effect of cultured Polyscias filcifolia Bailey cells on protein biosynthesis in an acellular system obtained from the liver of rabbits in experimental myocardial ischemia. It was found that the preparation normalizes the values of protein biosynthesis, the duration of the average polypeptide chain synthesis, and the activity of aminoacyl-tRNA synthetases.


Subject(s)
Liver/metabolism , Plants, Edible/cytology , Protein Biosynthesis , Animals , Cells, Cultured , Male , Rabbits
7.
Vopr Med Khim ; 36(5): 6-8, 1990.
Article in Russian | MEDLINE | ID: mdl-2251797

ABSTRACT

Properties of rabbit liver tissue aminoacyl-tRNA synthetases, associated with polyribosomes, were studied under conditions of normal state and within 12 hrs after simulation of myocardium infarction. Under conditions of myocardium infarction the activity of some forms of aminoacyl-tRNA synthetase was decreased in polyribosomes and protein fractions, liberated from polyribosomes by means of washing with buffer containing 0.5 M KCl. Polyribosomes stimulated the synthetases and protected them from heat inactivation. Deterioration of the synthetases interaction with polyribosomes appears to be among the factors responsible for impairment of protein biosynthesis under conditions of myocardium infarction.


Subject(s)
Amino Acyl-tRNA Synthetases/metabolism , Liver/metabolism , Polyribosomes/metabolism , Amino Acyl-tRNA Synthetases/antagonists & inhibitors , Animals , Enzyme Stability , Hot Temperature , Kinetics , Liver/enzymology , Male , Polyribosomes/enzymology , Rabbits
8.
Biull Eksp Biol Med ; 109(6): 563-5, 1990 Jun.
Article in Russian | MEDLINE | ID: mdl-2397292

ABSTRACT

Composition of high-molecular-weight aminoacyl-tRNA synthetases complexes from rabbit liver both in norm and after 12 h experimental myocardial ischemia (EMI) has been investigated. Partial redistribution of aminoacyl-tRNA synthetases activity from 1820 kD complex into 840 kD complex was observed in case of EMI which resulted in changes of protein biosynthesis rate in cell-free system.


Subject(s)
Amino Acyl-tRNA Synthetases/physiology , Coronary Disease/metabolism , Liver/metabolism , Protein Biosynthesis , Animals , Cell-Free System , Coronary Disease/enzymology , Male , Rabbits
9.
Vopr Med Khim ; 35(4): 56-60, 1989.
Article in Russian | MEDLINE | ID: mdl-2815681

ABSTRACT

Catalytic properties and thermostability of leucyl-tRNA-synthetase were studied both in free form and in the form of high molecular complexes, isolated from pig myocardium under normal state and after 15 min and 30 min ischemia. Km values of free and associated forms of leucyl-tRNA-synthetase were similar either in normal state or after 15-30 min ischemia. Complex-formation protected the enzyme from thermic inactivation under normal and ischemic conditions. Reverse redistribution of the leucyl-tRNA-synthetase activity was found in the fractions of free enzyme and high molecular complex depending on duration of ischemia.


Subject(s)
Amino Acyl-tRNA Synthetases/metabolism , Coronary Disease/enzymology , Leucine-tRNA Ligase/metabolism , Myocardium/enzymology , Animals , Catalysis , Hot Temperature , Kinetics , Swine
10.
Biokhimiia ; 54(3): 427-33, 1989 Mar.
Article in Russian | MEDLINE | ID: mdl-2665825

ABSTRACT

Comparative studies of the state of aggregation and activity of tRNA-methyltransferases in cytosol (105,000 X g supernatant) from normal and ischemic rabbit liver and myocardium were carried out. The optimal conditions (pH, protein concentration, ionic composition of incubation mixture) for the determination of activity of tRNA-methyltransferases were elaborated. The protein fraction precipitated at 55% saturation of ammonium sulfate was shown to inherit the highest activity of tRNA-methyltransferases. In rabbit liver cytosol, the bulk of the tRNA-methyltransferase activity (approximately 50%) was found to be associated with high molecular weight complexes containing aminoacyl-tRNA-synthetases. The tRNA-methyltransferase activity was increased almost 1.4-fold both in the myocardium cytosol under total ischemia of isolated heart (30 min, 37 degrees C) and in liver cytosol under experimental myocardial infarction (EMI, occlusion of anterior coronary artery for 12 hours). Moreover, the labilization of high molecular weight complexes was observed: up to 80% of the tRNA-methyltransferase activity was localized in the fraction of lower molecular weight complexes and free enzyme fraction. In the total set of eight methylated nucleotides (products of submethylated tRNA methylation by liver enzymes), the decreased m1A content and the increased m7G and m1G contents were observed at EMI. It was assumed that the observed changes in the state of aggregation of tRNA-methyltransferases, in particular, their dissociation from the high molecular weight amino-acyl-tRNA-synthetase complexes are prerequisites for the suppression of protein biosynthesis under ischemic conditions.


Subject(s)
Coronary Disease/enzymology , Ischemia/enzymology , Liver/enzymology , tRNA Methyltransferases/metabolism , Animals , Escherichia coli/enzymology , Hydrogen-Ion Concentration , Kinetics , Liver/blood supply , Male , Methylation , Molecular Weight , Rabbits
11.
Ukr Biokhim Zh (1978) ; 61(2): 34-8, 1989.
Article in Russian | MEDLINE | ID: mdl-2728111

ABSTRACT

Distribution of the aminoacyl-tRNA synthetase activity has been studied in the normal rabbit liver cells and in the model of protein synthesis damage, i.e. under experimental myocardial infarction (EMI). The activity of a number of aminoacyl-tRNA synthetases in postmitochondrial and postribosomal extracts from rabbit liver homogenate has been determined to increase 12 h after EMI. Gel filtration of the postribosomal extract on Sepharose 6B shows that the activity of aminoacyl-tRNA synthetases is distributed among the fractions with Mr 1.82 x 10(6), 0.84 x 10(6) and 0.12 = 0.35 x 10(6). The first two fractions (high-molecular-weight aminoacyl-tRNA synthetase complexes) contain arginyl-, glutamyl-, isoleucyl-, leucyl-, lysyl- and valyl-tRNA synthetases, whereas the low-molecular-weight fraction contains alanyl-, arginyl-, glycyl-, phenylalanyl-, seryl-, threonyl-, tryptophanyl- and tyrosyl-tRNA synthetases. In a case of EMI all the aminoacyl-tRNA synthetases translocate from the complexes with Mr 1.82 x 10(6) into the complexes with Mr 0.84 x 10(6), what provided evidence for the possibility to regulate protein synthesis by changes in compartmentalization of aminoacyl-tRNA synthetases.


Subject(s)
Amino Acyl-tRNA Synthetases/metabolism , Liver/enzymology , Myocardial Infarction/enzymology , Protein Biosynthesis , Animals , Chromatography, Gel , Liver/metabolism , Myocardial Infarction/metabolism , Rabbits
12.
Vopr Med Khim ; 34(2): 84-6, 1988.
Article in Russian | MEDLINE | ID: mdl-3400198

ABSTRACT

Distinct decrease in the rate of aminoacylation of tRNAs, specific to alanine, glutamic acid, leucine and serine, was found after 20 min anoxia of perfused pig heart. In the anoxia activity of aminoacyl-tRNA synthetases of the same amino acid specificity was increased. Reduction of these macromolecules activity was observed in reoxygenation of the anoxic myocardium. Biological activity of tRNA and aminoacyl-tRNA synthetases in pig myocardium appears to depend on the supply of heart with oxygen.


Subject(s)
Amino Acyl-tRNA Synthetases/metabolism , Myocardium/metabolism , Oxygen/pharmacology , RNA, Transfer/metabolism , Animals , In Vitro Techniques , Myocardium/enzymology , Protein Biosynthesis , Swine
13.
Ukr Biokhim Zh (1978) ; 58(6): 15-22, 1986.
Article in Russian | MEDLINE | ID: mdl-3798576

ABSTRACT

The catalytical properties and thermostability of free leucyl-, glutamyl- and lysyl-tRNA synthetases and of the same synthetases in codosomes are compared. The stability of different aminoacyl-tRNA synthetases in highly purified preparations and in codosomes did not submit to any common regularities. Km for all substrates both for purified and assembled ARSases are values of the same order. It is shown in some model systems that the aminoacyl-tRNA synthetase activity in codosomes depends on the presence of pyrophosphatase. Other important components of codosomes are protein kinases and phospholipids which are able to influence the aminoacyl-tRNA synthetase activity and structural organization.


Subject(s)
Amino Acyl-tRNA Synthetases/analysis , Amino Acyl-tRNA Synthetases/antagonists & inhibitors , Animals , Electrophoresis, Polyacrylamide Gel , Eukaryotic Cells , Kinetics , Liver/enzymology , Macromolecular Substances , Myocardium/enzymology , Rabbits , Rats , Rats, Inbred Strains , Swine , Temperature
14.
Vopr Med Khim ; 31(5): 104-7, 1985.
Article in Russian | MEDLINE | ID: mdl-3004032

ABSTRACT

In pig myocardial extracts autolyzed within 15 min alanyl-, glycyl-, glutamyl-, leucyl- and seryl-tRNA synthetase activities were increased as compared with controls. The enzymatic activities were decreased after autolysis for 30 min. The 15 min autolysis was shown to decrease the molecular mass of the glycyl-tRNA synthetase complex. Within both 15 min and 30 min autolysis inorganic pyrophosphatase was markedly activated either in myocardium extracts or in high molecular complexes; this phenomenon may be responsible for activation of a number of aminoacyl-tRNA synthetases.


Subject(s)
Amino Acyl-tRNA Synthetases/metabolism , Autolysis/enzymology , Coronary Disease/enzymology , Myocardium/enzymology , Amino Acids/metabolism , Animals , Coronary Disease/pathology , In Vitro Techniques , Inorganic Pyrophosphatase , Molecular Weight , Myocardium/pathology , Pyrophosphatases/metabolism , Swine
15.
Mol Biol (Mosk) ; 18(5): 1326-9, 1984.
Article in Russian | MEDLINE | ID: mdl-6150436

ABSTRACT

A number of aminoacyl-tRNA synthetases from rabbit liver during experimental myocardial infarction and from pig myocardium upon 15-min of autolysis were found to increase their activity in aminoacylation. Direct correlations between the activities of high molecular weight complexes and of the total extracts were not observed. It was shown that the specific activity of endogenous inorganic pyrophosphatase increased markedly during the ischemia of myocardium both in total myocardium extracts and in high molecular weight complexes.


Subject(s)
Amino Acyl-tRNA Synthetases/metabolism , Coronary Disease/enzymology , Liver/enzymology , Myocardium/enzymology , Animals , Autolysis/enzymology , In Vitro Techniques , Molecular Weight , Myocardial Infarction/enzymology , Pyrophosphatases/metabolism , Rabbits , Swine
16.
Ukr Biokhim Zh (1978) ; 55(4): 368-71, 1983.
Article in Russian | MEDLINE | ID: mdl-6623664

ABSTRACT

The composition of high-molecular complexes of aminoacyl-tRNA-synthetases (ARSase) from the rabbit liver was studied on the first day after reproduction of the experimental myocardium infarction. The studies revealed an increase in the glutamyl-, leucyl-, lysyl- and a decrease in the glycyl- and seryl-tRNA-synthetase activities and redistribution of the last two enzymes from the composition of the complexes into a lower-molecular fraction of postribosomal supernatant fluid. Under the experimental myocardium infarction the complexes reveal a significant decrease in the content of phospholipids and variations in the electrophoretic mobility of protein fractions. An assumption is advanced that a disturbed protein biosynthesis in the liver resulted from the experimental myocardium infarction causes changes in the structural organization of the ARSase complexes.


Subject(s)
Amino Acyl-tRNA Synthetases/metabolism , Liver/enzymology , Myocardial Infarction/enzymology , Animals , Chromatography, Ion Exchange , Molecular Weight , Rabbits , Time Factors
17.
Ukr Biokhim Zh (1978) ; 54(3): 322-5, 1982.
Article in Russian | MEDLINE | ID: mdl-7101478

ABSTRACT

P-chloromercuribenzoate (PCMB) inhibition of the leucyl-t-RNA-synthetase (LeuRS) activity was studied both in the tRNA-aminoacylation and ATP-[32P]-pyrophosphate exchange reactions. It is established that the enzyme contained sulphydryl (SH) groups essential for catalytic activity. No protection of substrates from the PCMB action was observed in both reactions. It is shown that SH-groups essential for tRNA-aminoacylation were of no use for leucine activation. The PCMB modified enzyme was reactivated (80%) after the treatment with dithiothreitol. The quantity of cysteine residues in the native and denatured forms of LeuRS was determined.


Subject(s)
Amino Acyl-tRNA Synthetases/antagonists & inhibitors , Chloromercuribenzoates/pharmacology , Leucine-tRNA Ligase/antagonists & inhibitors , Mammary Glands, Animal/enzymology , Animals , Cattle , Female , Kinetics , Sulfhydryl Compounds/analysis , p-Chloromercuribenzoic Acid
18.
Mol Biol (Mosk) ; 13(3): 550-8, 1979.
Article in Russian | MEDLINE | ID: mdl-572475

ABSTRACT

Three forms (E1, E2 and E3) of leucyl-tRNA synthetase (LeuRS) were separated by DEAE-cellulose chromatography of total aminoacyl-tRNA synthetases from cow lactating mammary gland. The method of purification of all three components is described. E1 is a dimeric molecule (alpha 2) of molecular weight 182 000. Two other forms of molecular weight 67 000 and 64,000 consist of a single polypeptide chain as determined by polyacrylamide gel electrophoresis. Optimum conditions and kinetic parameters of leucyl-tRNA formation were studied for every enzyme form. The low values of Vmax and thermostability are characteristic of E3. All forms of LeuRS interact with 6 isoaccepting tRNA(Leu) from lactating mammary gland and can activate leucine in the absence of tRNA. E2 and E3 are supposed to derive from the native enzyme by endogenous proteolysis. The physico-chemical properties of native LeuRS from lactating mammary gland are compared with those of LeuRS's from other sources.


Subject(s)
Amino Acyl-tRNA Synthetases/metabolism , Leucine-tRNA Ligase/metabolism , Mammary Glands, Animal/enzymology , Animals , Cattle , Female , Isoenzymes/isolation & purification , Isoenzymes/metabolism , Kinetics , Lactation , Leucine-tRNA Ligase/isolation & purification , Molecular Weight , Pregnancy
19.
Biokhimiia ; 43(3): 525-34, 1978 Mar.
Article in Russian | MEDLINE | ID: mdl-656489

ABSTRACT

The interaction between tryptophanyl-tRNA synthetase (EC 6.1.1.2) from beef pancreas and the ATP analogs containing alkylating or phosphorylating groups in the polyphosphate moiety of ATP was studied as an approach to investigate the structure of the enzyme active center. Some of the compounds under study were shown to irreversibly inhibit the enzyme activity; the presence of ATP in the most cases protects the enzyme against inactivation. The kinetic constants Ki and k2 of interaction of the irreversible inhibitors with the enzyme were determined. It was found that the Ki values for a number of irreversible competitive inhibitors are by 1-2 orders of magnitude less than the Km value for ATP; the k2 values were found equal to 0.02-0.04 min-1. this suggests that the compounds may be used as affinity reagents, the most efficient ones being adenosine 5'-(beta-chloroethyl phosphate) and mixed AMP-mesithylene carbonic acid anhydride. The absence of a protective effect of ATP in the case of adenosine 5'-(beta-bromoethane phosphonate) and non-competitive type of reversible inhibition inhibition of the enzyme by adenosine 5'-chloromethane phosphonate indicate that the molecule of tryptophanyl-tRNA synthetase contains sites interacting with adenine nucleotides, other than the ATP binding sites of the active center.


Subject(s)
Adenosine Triphosphate/analogs & derivatives , Amino Acyl-tRNA Synthetases/antagonists & inhibitors , Tryptophan-tRNA Ligase/antagonists & inhibitors , Animals , Cattle , Kinetics , Pancreas/enzymology , Structure-Activity Relationship
20.
Biokhimiia ; 41(4): 619-29, 1976 Apr.
Article in Russian | MEDLINE | ID: mdl-1022288

ABSTRACT

The course of stereospecific selection of nucleophilic compounds was studied in the reaction of acyl-enzymes interaction with razemic substrate-like nucleophiles, e.g. amino acid esters, by measuring optical rotation or incorporation of labelled D-compounds. It was shown that the acyl-enzymes are not responsible for the stereospecific selection of substrate-like nucleophiles. Since stereospecific selection of nucleophiles occurs in some chymotrypsin-catalyzed reactions, such selection may be produced by chymotrypsin till the formation of an acyl-enzyme compound with the substrate at the enzyme-inhibitor stage (or the Michaelis complex) with nucleophilic compounds. Even under the optimal conditions no absolute stereospecific selection of nucleophiles occurred, as was observed in case of a substrate (a donor of the acyl amino acid residue), undergoing degradation. An essential role of a specific site of nucleophile binding in the reactions of chymotrypsin-catalyzed peptide bond formation, is emphasized.


Subject(s)
Chymotrypsin/metabolism , Peptide Biosynthesis , Amino Acids/metabolism , Binding Sites , Chymotrypsin/antagonists & inhibitors , Structure-Activity Relationship
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